Structure of PDB 4axa Chain A Binding Site BS02

Receptor Information
>4axa Chain A (length=337) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHM
ETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLTKLEFSFKDN
SNLYMVMEYAPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLI
YRDLKPENLMIDQQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSK
GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSS
DLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAP
FIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Ligand information
Ligand IDRKD
InChIInChI=1S/C17H16ClN3O/c18-16-7-5-15(6-8-16)17(22,11-19)14-3-1-12(2-4-14)13-9-20-21-10-13/h1-10,22H,11,19H2,(H,20,21)/p+1/t17-/m0/s1
InChIKeyIIRWNGPLJQXWFJ-KRWDZBQOSA-O
SMILES
SoftwareSMILES
CACTVS 3.370[NH3+]C[C](O)(c1ccc(Cl)cc1)c2ccc(cc2)c3c[nH]nc3
OpenEye OEToolkits 1.7.6c1cc(ccc1c2c[nH]nc2)C(C[NH3+])(c3ccc(cc3)Cl)O
OpenEye OEToolkits 1.7.6c1cc(ccc1c2c[nH]nc2)[C@@](C[NH3+])(c3ccc(cc3)Cl)O
ACDLabs 12.01Clc1ccc(cc1)C(O)(c3ccc(c2cnnc2)cc3)C[NH3+]
CACTVS 3.370[NH3+]C[C@@](O)(c1ccc(Cl)cc1)c2ccc(cc2)c3c[nH]nc3
FormulaC17 H17 Cl N3 O
Name(2S)-2-(4-chlorophenyl)-2-hydroxy-2-[4-(1H-pyrazol-4-yl)phenyl]ethanaminium;
(1S)-2-AMINO-1-(4-CHLOROPHENYL)-1-(4-(1H-PYRAZOL-4-YL)PHENYL)ETHAN-1-OL
ChEMBL
DrugBank
ZINC
PDB chain4axa Chain A Residue 1351 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4axa At13148 is a Novel, Oral Multi-Agc Kinase Inhibitor with Potent Pharmacodynamic and Antitumor Activity.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G50 T51 G55 R56 V57 A70 K72 E121 Y122 E127 E170 N171 M173 T183 D184
Binding residue
(residue number reindexed from 1)		G37 T38 G42 R43 V44 A57 K59 E108 Y109 E114 E157 N158 M160 T170 D171
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.00,IC50<10nM
Enzymatic activity
Catalytic site (original residue number in PDB) D166 K168 E170 N171 D184 T201
Catalytic site (residue number reindexed from 1) D153 K155 E157 N158 D171 T188
Enzyme Commision number 2.7.11.11: cAMP-dependent protein kinase.
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004679 AMP-activated protein kinase activity
GO:0004691 cAMP-dependent protein kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0019904 protein domain specific binding
GO:0034237 protein kinase A regulatory subunit binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0001707 mesoderm formation
GO:0006468 protein phosphorylation
GO:0010737 protein kinase A signaling
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0034605 cellular response to heat
GO:1904262 negative regulation of TORC1 signaling
Cellular Component
GO:0001669 acrosomal vesicle
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005952 cAMP-dependent protein kinase complex
GO:0031594 neuromuscular junction
GO:0036126 sperm flagellum
GO:0048471 perinuclear region of cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4axa, PDBe:4axa, PDBj:4axa
PDBsum4axa
PubMed22781553
UniProtP00517|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

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