STYKcProtein kinase; unclassified specificity.
|SMART accession number:||SM00221|
|Description:||Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.|
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- Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with STYKc domain is also avaliable.
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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Engh RA, Girod A, Kinzel V, Huber R, Bossemeyer D
- Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity.
- J Biol Chem. 1996; 271: 26157-64
- Display abstract
The discovery of several hundred different protein kinases involved in highly diverse cellular signaling pathways is in stark contrast to the much smaller number of known modulators of cell signaling. Of these, the H series protein kinase inhibitors (1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H7), N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide (H8) N-[2-(p-Bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H89)) are frequently used to block signaling pathways in studies of cellular regulation. To elucidate inhibition mechanisms at atomic resolution and to enable structure-based drug design of potential therapeutic modulators of signaling pathways, we determined the crystal structures of corresponding complexes with the cAPK catalytic subunit. Complexes with H7 and H8 (2.2 A) and with H89 (2.3 A) define the binding mode of the isoquinoline-sulfonamide derivatives in the ATP-binding site while demonstrating effects of ligand-induced structural change. Specific interactions between the enzyme and the inhibitors include the isoquinoline ring nitrogen ligating to backbone amide of Val-123 and an inhibitor side chain amide bonding to the backbone carbonyl of Glu-170. The conservation of the ATP-binding site of protein kinases allows evaluation of factors governing general selectivity of these inhibitors among kinases. These results should assist efforts in the design of protein kinase inhibitors with specific properties.
- Mohammadi M, Schlessinger J, Hubbard SR
- Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism.
- Cell. 1996; 86: 577-87
- Display abstract
The crystal structure of the tyrosine kinase domain of fibroblast growth factor receptor 1 (FGFR1K) has been determined in its unliganded form to 2.0 angstroms resolution and in complex with with an ATP analog to 2.3 angstrosms A resolution. Several features distinguish the structure of FGFR1K from that of the tyrosine kinase domain of the insulin receptor. Residues in the activation loop of FGFR1K appear to interfere with substrate peptide binding but not with ATP binding, revealing a second and perhaps more general autoinhibitory mechanism for receptor tyrosine kinases. In addition, a dimeric form of FGFR1K observed in the crystal structure may provide insights into the molecular mechanisms by which FGF receptors are activated. Finally, the structure provides a basis for rationalizing the effects of kinase mutations in FGF receptors that lead to developmental disorders in nematodes and humans.
- Hanks SK, Hunter T
- Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.
- FASEB J. 1995; 9: 576-96
- Display abstract
The eukaryotic protein kinases make up a large superfamily of homologous proteins. They are related by virtue of their kinase domains (also known as catalytic domains), which consist of approximately 250-300 amino acid residues. The kinase domains that define this group of enzymes contain 12 conserved subdomains that fold into a common catalytic core structure, as revealed by the 3-dimensional structures of several protein-serine kinases. There are two main subdivisions within the superfamily: the protein-serine/threonine kinases and the protein-tyrosine kinases. A classification scheme can be founded on a kinase domain phylogeny, which reveals families of enzymes that have related substrate specificities and modes of regulation.
- Owen DJ, Noble ME, Garman EF, Papageorgiou AC, Johnson LN
- Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.
- Structure. 1995; 3: 467-82
- Display abstract
BACKGROUND: Control of intracellular events by protein phosphorylation is promoted by specific protein kinases. All the known protein kinase possess a common structure that defines a catalytically competent entity termed the 'kinase catalytic core'. Within this common structural framework each kinase displays its own unique substrate specificity, and a regulatory mechanism that may be modulated by association with other proteins. Structural studies of phosphorylase kinase (Phk), the major substrate of which is glycogen phosphorylase, may be expected to shed light on its regulation. RESULTS: We report two crystal structures of the catalytic core (residues 1-298; Phk gamma trnc) of the gamma-subunit of rabbit muscle phosphorylase kinase: the binary complex with Mn2+/beta-gamma-imidoadenosine 5'-triphosphate (AMPPNP) to a resolution of 2.6 A and the binary complex with Mg2+/ADP to a resolution of 3.0 A. The structures were solved by molecular replacement using the cAMP-dependent protein kinase (cAPK) as a model. CONCLUSIONS: The overall structure of Phk gamma trnc is similar to that of the catalytic core of other protein kinases. It consists of two domians joined on one edge by a 'hinge', with the catalytic site located in the cleft between the domains. Phk gamma trnc is constitutively active, and lacks the need for an activatory phosphorylation event that is essential for many kinases. The structure exhibits an essentially 'closed' conformation of the domains which is similar to that of cAPK complexed with substrates. The phosphorylated residue that is located at the domain interface in many protein kinases and that is believed to stabilize an active conformation is substituted by a glutamate in Phk gamma trnc. The glutamate, in a similar manner to the phosphorylated residue in other protein kinases, interacts with an arginine adjacent to the catalytic aspartate but does not participate in interdomain contacts. The interactions between the enzyme and the nucleotide product of its activity, Mg2+/ADP, explain the inhibitory properties of the nucleotides that are observed in kinetic studies.
- Schulze-Gahmen U et al.
- Multiple modes of ligand recognition: crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine.
- Proteins. 1995; 22: 378-91
- Display abstract
Cyclin-dependent kinases (CDKs) are conserved regulators of the eukaryotic cell cycle with different isoforms controlling specific phases of the cell cycle. Mitogenic or growth inhibitory signals are mediated, respectively, by activation or inhibition of CDKs which phosphorylate proteins associated with the cell cycle. The central role of CDKs in cell cycle regulation makes them a potential new target for inhibitory molecules with anti-proliferative and/or anti-neoplastic effects. We describe the crystal structures of the complexes of CDK2 with a weakly specific CDK inhibitor, N6-(delta 2-isopentenyl)adenine, and a strongly specific inhibitor, olomoucine. Both inhibitors are adenine derivatives and bind in the adenine binding pocket of CDK2, but in an unexpected and different orientation from the adenine of the authentic ligand ATP. The N6-benzyl substituent in olomoucine binds outside the conserved binding pocket and is most likely responsible for its specificity. The structural information from the CDK2-olomoucine complex will be useful in directing the search for the next generation inhibitors with improved properties.
- Zhang J, Zhang F, Ebert D, Cobb MH, Goldsmith EJ
- Activity of the MAP kinase ERK2 is controlled by a flexible surface loop.
- Structure. 1995; 3: 299-307
- Display abstract
BACKGROUND: The mitogen-activated protein (MAP) kinase, ERK2, is a tightly regulated enzyme in the ubiquitous Ras-activated protein kinase cascade. ERK2 is activated by phosphorylation at two sites, Y185 and T183, that lie in the phosphorylation lip at the mouth of the catalytic site. To ascertain the role of these two residues in securing the low-activity conformation of the enzymes we have carried out crystallographic analyses and assays of phosphorylation-site mutants of ERK2. RESULTS: The crystal structures of four mutants, T183E (threonine at residue 183 is replaced by glutamate), Y185E, Y185F and the double mutant T183E/Y185E, were determined. When T183 is replaced by glutamate, few conformational changes are observed. By contrast, when Y185 is replaced by glutamate, 19 residues become disordered, including the entire phosphorylation lip and an adjacent loop. The conservative substitution of phenylalanine for Y185 also induces relatively large conformational changes. A binding site for phosphotyrosine in the active enzyme is putatively identified on the basis of the high-resolution refinement of the structure of wild-type ERK2. CONCLUSIONS: The remarkable disorder observed throughout the phosphorylation lip when Y185 is mutated shows that the stability of the phosphorylation lip is rather low. Therefore, only modest amounts of binding energy will be required to dislodge the lip for phosphorylation, and it is likely that these residues will be involved in conformational changes associated with both with binding to kinases and phosphatases and with activation. Furthermore, the low-activity structure is specifically dependent on Y185, whereas there is no such dependency on T183. Both residues, however, participate in forming the active enzyme, contributing to its tight control.
- Hubbard SR, Wei L, Ellis L, Hendrickson WA
- Crystal structure of the tyrosine kinase domain of the human insulin receptor.
- Nature. 1994; 372: 746-54
- Display abstract
The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 A resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.
- Taylor SS, Radzio-Andzelm E
- Three protein kinase structures define a common motif.
- Structure. 1994; 2: 345-55
- Display abstract
Structural comparisons between cAMP-dependent protein kinase, cyclin-dependent kinase 2 and mitogen-activated protein kinase reveal which features are common to the protein kinase family and which are enzyme-specific.
- Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ
- Atomic structure of the MAP kinase ERK2 at 2.3 A resolution.
- Nature. 1994; 367: 704-11
- Display abstract
The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.
- Bossemeyer D, Engh RA, Kinzel V, Ponstingl H, Huber R
- Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24).
- EMBO J. 1993; 12: 849-59
- Display abstract
The crystal structure of the porcine heart catalytic subunit of cAMP-dependent protein kinase in a ternary complex with the MgATP analogue MnAMP-PNP and a pseudosubstrate inhibitor peptide, PKI(5-24), has been solved at 2.0 A resolution from monoclinic crystals of the catalytic subunit isoform CA. The refinement is presently at an R factor of 0.194 and the active site of the molecule is well defined. The glycine-rich phosphate anchor of the nucleotide binding fold motif of the protein kinase is a beta ribbon acting as a flap with conformational flexibility over the triphosphate group. The glycines seem to be conserved to avoid steric clash with ATP. The known synergistic effects of substrate binding can be explained by hydrogen bonds present only in the ternary complex. Implications for the kinetic scheme of binding order are discussed. The structure is assumed to represent a phosphotransfer competent conformation. The invariant conserved residue Asp166 is proposed to be the catalytic base and Lys168 to stabilize the transition state. In some tyrosine kinases Lys168 is functionally replaced by an Arg displaced by two residues in the primary sequence, suggesting invariance in three-dimensional space. The structure supports an in-line transfer with a pentacoordinate transition state at the phosphorus with very few nuclear movements.
- DeBondt HL, Rosenblatt J, Jancarik J, Jones HD, Morgan DO, Kim SH
- Crystal structure of cyclin-dependent kinase 2.
- Nature. 1993; 363: 595-602
- Display abstract
Cyclin-dependent kinase 2 (CDK2) is a member of a highly conserved family of protein kinases that regulate the eukaryotic cell cycle. The crystal structures of the human CDK2 apoenzyme and its Mg2+ ATP complex have been determined to 2.4 A resolution. The structure is bi-lobate, like that of the cyclic AMP-dependent protein kinase, but contains a unique helix-loop segment that interferes with ATP and protein substrate binding and probably plays a key part in the regulation of all cyclin-dependent kinases.
- Zheng J et al.
- Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor.
- Biochemistry. 1993; 32: 2154-61
- Display abstract
The structure of a ternary complex of the catalytic subunit of cAMP-dependent protein kinase, MgATP, and a 20-residue inhibitor peptide was determined at a resolution of 2.7 A using the difference Fourier technique starting from the model of the binary complex (Knighton et al., 1991a). The model of the ternary complex was refined using both X-PLOR and TNT to an R factor of 0.212 and 0.224, respectively. The orientation of the nucleotide and the interactions of MgATP with numerous conserved residues at the active site of the enzyme are clearly defined. The unique protein kinase nucleotide binding site consists of a five-stranded antiparallel beta-sheet with the base buried in a hydrophobic site along beta-strands 1 and 2 and fixed by hydrogen bonds to the N6 amino and N7 nitrogens. The small lobe secures the nucleotide via a glycine-rich loop and by ion pairing with Lys72 and Glu91. While the small lobe fixes the nontransferable alpha- and beta-phosphates in this inhibitor complex, the gamma-phosphate is secured by two Mg2+ ions and interacts both directly and indirectly with several residues in the large lobe--Asp184, Asn171, Lys168. Asp166 is positioned to serve as a catalytic base. The structure is correlated with previous chemical evidence, and the features that distinguish this nucleotide binding motif from other nucleotide binding proteins are delineated.
- Knighton DR, Zheng JH, TenEyck LF, Xuong NH, Taylor SS, Sowadski JM
- Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
- Science. 1991; 253: 414-20
- Display abstract
The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area.
- Knighton DR et al.
- Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
- Science. 1991; 253: 407-14
- Display abstract
The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 9.26 map00632 Benzoate degradation via CoA ligation 9.26 map00562 Inositol phosphate metabolism 4.59 map04010 MAPK signaling pathway 3.80 map04060 Cytokine-cytokine receptor interaction 3.80 map04350 TGF-beta signaling pathway 3.24 map04620 Toll-like receptor signaling pathway 3.05 map04730 Long-term depression 3.01 map04540 Gap junction 2.81 map04340 Hedgehog signaling pathway 2.65 map05212 Pancreatic cancer 2.61 map05220 Chronic myeloid leukemia 2.49 map04210 Apoptosis 2.37 map04110 Cell cycle 2.37 map00130 Ubiquinone biosynthesis 2.18 map00230 Purine metabolism 2.14 map04914 Progesterone-mediated oocyte maturation 2.10 map04810 Regulation of actin cytoskeleton 2.10 map05210 Colorectal cancer 1.94 map04520 Adherens junction 1.94 map04111 Cell cycle - yeast 1.82 map04920 Adipocytokine signaling pathway 1.42 map04310 Wnt signaling pathway 1.42 map04910 Insulin signaling pathway 1.42 map05215 Prostate cancer 1.38 map05221 Acute myeloid leukemia 1.27 map04012 ErbB signaling pathway 1.23 map04660 T cell receptor signaling pathway 1.19 map05213 Endometrial cancer 1.19 map04510 Focal adhesion 1.15 map04630 Jak-STAT signaling pathway 1.07 map04360 Axon guidance 1.03 map04140 Regulation of autophagy 1.03 map05214 Glioma 0.99 map05120 Epithelial cell signaling in Helicobacter pylori infection 0.95 map04720 Long-term potentiation 0.95 map04530 Tight junction 0.95 map05219 Bladder cancer 0.95 map05223 Non-small cell lung cancer 0.91 map05211 Renal cell carcinoma 0.91 map05218 Melanoma 0.87 map04150 mTOR signaling pathway 0.87 map04650 Natural killer cell mediated cytotoxicity 0.71 map04912 GnRH signaling pathway 0.67 map04664 Fc epsilon RI signaling pathway 0.59 map05222 Small cell lung cancer 0.55 map04662 B cell receptor signaling pathway 0.47 map04370 VEGF signaling pathway 0.47 map04710 Circadian rhythm 0.44 map04930 Type II diabetes mellitus 0.44 map04916 Melanogenesis 0.32 map04020 Calcium signaling pathway 0.32 map03320 PPAR signaling pathway 0.28 map05216 Thyroid cancer 0.20 map05020 Parkinson's disease 0.12 map00540 Lipopolysaccharide biosynthesis 0.12 map04670 Leukocyte transendothelial migration 0.08 map00350 Tyrosine metabolism 0.08 map04740 Olfactory transduction 0.08 map02020 Two-component system - General 0.08 map00150 Androgen and estrogen metabolism 0.08 map00626 Naphthalene and anthracene degradation 0.08 map04115 p53 signaling pathway 0.08 map00271 Methionine metabolism 0.08 map00361 gamma-Hexachlorocyclohexane degradation 0.08 map00360 Phenylalanine metabolism 0.08 map00380 Tryptophan metabolism 0.08 map00643 Styrene degradation 0.08 map00622 Toluene and xylene degradation 0.08 map00627 1,4-Dichlorobenzene degradation 0.08 map00340 Histidine metabolism 0.08 map00120 Bile acid biosynthesis 0.08 map00363 Bisphenol A degradation 0.08 map00680 Methane metabolism 0.08 map00903 Limonene and pinene degradation 0.08 map00624 1- and 2-Methylnaphthalene degradation 0.04 map05217 Basal cell carcinoma 0.04 map04070 Phosphatidylinositol signaling system 0.04 map04320 Dorso-ventral axis formation 0.04 map05050 Dentatorubropallidoluysian atrophy (DRPLA)
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with STYKc domain which could be assigned to a KEGG orthologous group, and not all proteins containing STYKc domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of STYKc domains in PDB
PDB code Main view Title 1b6c Crystal structure of the cytoplasmic domain of the type i tgf-beta receptor in complex with fkbp12 1cki Recombinant casein kinase i delta truncation mutant containing residues 1-317 1ckj Casein kinase i delta truncation mutant containing residues 1-317 complex with bound tungstate 1csn Binary complex of casein kinase-1 with mgatp 1eh4 Binary complex of casein kinase-1 from s. pombe with an atp competitive inhibitor, ic261 1ias Cytoplasmic domain of unphosphorylated type i tgf-beta receptor crystallized without fkbp12 1py5 Crystal structure of tgf-beta receptor i kinase with inhibitor 1rw8 Crystal structure of tgf-beta receptor i kinase with atp site inhibitor 1uwh The complex of wild type b-raf and bay439006 1uwj The complex of mutant v599e b-raf and bay439006 1vjy Crystal structure of a naphthyridine inhibitor of human tgf- beta type i receptor 1wak X-ray structure of srpk1 1wbp Srpk1 bound to 9mer docking motif peptide 1x8b Structure of human wee1a kinase: kinase domain complexed with inhibitor pd0407824 2a19 Pkr kinase domain- eif2alpha- amp-pnp complex. 2a1a Pkr kinase domain-eif2alpha complex 2buj Crystal structure of the human serine-threonine kinase 16 in complex with staurosporine 2c47 Structure of casein kinase 1 gamma 2 2chl Structure of casein kinase 1 gamma 3 2cmw Structure of human casein kinase 1 gamma-1 in complex with 2-(2-hydroxyethylamino)-6-(3-chloroanilino)-9- isopropylpurine (casp target) 2csn Binary complex of casein kinase-1 with cki7 2eva Structural basis for the interaction of tak1 kinase with its activating protein tab1 2fb8 Structure of the b-raf kinase domain bound to sb-590885 2h34 Apoenzyme crystal structure of the tuberculosis serine/threonine kinase, pkne 2in6 Wee1 kinase complex with inhibitor pd311839 2io6 Wee1 kinase complexed with inhibitor pd330961 2izr Structure of casein kinase gamma 3 in complex with inhibitor 2izs Structure of casein kinase gamma 3 in complex with inhibitor 2izt Structure of casein kinase gamma 3 in complex with inhibitor 2izu Structure of casein kinase gamma 3 in complex with inhibitor 2jii Structure of vaccinia related kinase 3 2nru Crystal structure of irak-4 2nry Crystal structure of irak-4 2o8y Apo irak4 kinase domain 2oib Crystal structure of irak4 kinase domain apo form 2oic Crystal structure of irak4 kinase domain complexed with staurosporine 2oid Crystal structure of irak4 kinase domain complexed with amppnp 2pml Crystal structure of pfpk7 in complex with an atp analogue 2pmn Crystal structure of pfpk7 in complex with an atp-site inhibitor 2pmo Crystal structure of pfpk7 in complex with hymenialdisine 2pzi Crystal structure of protein kinase pkng from mycobacterium tuberculosis in complex with tetrahydrobenzothiophene ax20017 2qkw Structural basis for activation of plant immunity by bacterial effector protein avrpto 2qlu Crystal structure of activin receptor type ii kinase domain from human 2rio Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation of non-conventional splicing 2v62 Structure of vaccinia-related kinase 2 2vuw Structure of human haspin kinase domain 2vwb Structure of the archaeal kae1-bud32 fusion protein mj1130: a model for the eukaryotic ekc-keops subcomplex involved in transcription and telomere homeostasis. 2w1z Rop2 from toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity. 2wb8 Crystal structure of haspin kinase 2wot Alk5 in complex with 4-((5,6-dimethyl-2-(2-pyridyl)-3- pyridyl)oxy)-n-(3,4,5-trimethoxyphenyl)pyridin-2-amine 2wou Alk5 in complex with 4-((4-((2,6-dimethyl-3-pyridyl)oxy)-2- pyridyl)amino)benzenesulfonamide 2z2w Humand wee1 kinase complexed with inhibitor pf0335770 3beg Crystal structure of sr protein kinase 1 complexed to its substrate asf/sf2 3bi6 Wee1 kinase complex with inhibitor pd352396 3biz Wee1 kinase complex with inhibitor pd331618 3byv Crystal structure of toxoplasma gondii specific rhoptry antigen kinase domain 3c4c B-raf kinase in complex with plx4720 3c4d B-raf kinase v600e oncogenic mutant in complex with plx3203 3cqe Wee1 kinase complex with inhibitor pd074291 3cr0 Wee1 kinase complex with inhibitor pd259_809 3d4q Pyrazole-based inhibitors of b-raf kinase 3dlz Crystal structure of human haspin in complex with amp 3dzo Crystal structure of a rhoptry kinase from toxoplasma gondii 3e7e Structure and substrate recruitment of the human spindle checkpoint kinase bub 3e7v Crystal structure of human haspin with a pyrazolo- pyrimidine ligand 3en9 Structure of the methanococcus jannaschii kae1-bud32 fusion protein 3enh Crystal structure of cgi121/bud32/kae1 complex 3f2n Crystal structure of human haspin with an imidazo- pyridazine ligand 3faa Crystal structure of tgfbri complexed with a 2- aminoimidazole inhibitor 3fbv Crystal structure of the oligomer formed by the kinase- ribonuclease domain of ire1 3fmd Crystal structure of human haspin with an isoquinoline ligand 3fpq Crystal structure of the kinase domain of wnk1 3g2f Crystal structure of the kinase domain of bone morphogenetic protein receptor type ii (bmpr2) at 2.35 a resolution 3gni Structure of strad and mo25 3gxl Alk-5 kinase complex with gw857175 3h9r Crystal structure of the kinase domain of type i activin receptor (acvr1) in complex with fkbp12 and dorsomorphin 3hgk Crystal structure of effect protein avrptob complexed with kinase pto 3hmm Structure of alk5 + gw855857 3idp B-raf v600e kinase domain in complex with an aminoisoquinoline inhibitor 3ii5 The complex of wild-type b-raf with pyrazolo pyrimidine inhibitor 3iq7 Crystal structure of human haspin in complex with 5- iodotubercidin