Structure of PDB 4c35 Chain A Binding Site BS02

Receptor Information
>4c35 Chain A (length=341) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSYGRVML
VKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFS
FKDNSNLYMVLEYLPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS
LDLIYRDLKPENLMIDQQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEI
ILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS
HFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRK
VEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Ligand information
Ligand IDNU3
InChIInChI=1S/C14H11N3O2/c15-13(19)10-2-1-3-11-12(10)17-14(16-11)8-4-6-9(18)7-5-8/h1-7,18H,(H2,15,19)(H,16,17)
InChIKeyKOUGHMOSYJCJLE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1cc(c2c(c1)[nH]c(n2)c3ccc(cc3)O)C(=O)N
ACDLabs 12.01O=C(c3cccc2c3nc(c1ccc(O)cc1)n2)N
CACTVS 3.385NC(=O)c1cccc2[nH]c(nc12)c3ccc(O)cc3
FormulaC14 H11 N3 O2
Name2-(4-hydroxyphenyl)-1H-benzimidazole-4-carboxamide
ChEMBLCHEMBL131719
DrugBank
ZINCZINC000000026019
PDB chain4c35 Chain A Residue 1351 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4c35 The discovery of potent ribosomal S6 kinase inhibitors by high-throughput screening and structure-guided drug design.
Resolution2.19 Å
Binding residue
(original residue number in PDB)		V57 A70 K72 E91 L95 V104 L120 Y122 L123 M173 T183 D184 F327
Binding residue
(residue number reindexed from 1)		V48 A61 K63 E82 L86 V95 L111 Y113 L114 M164 T174 D175 F318
Annotation score1
Binding affinityMOAD: ic50=0.56uM
PDBbind-CN: -logKd/Ki=6.25,IC50=0.56uM
Enzymatic activity
Catalytic site (original residue number in PDB) D166 K168 E170 N171 D184 T201
Catalytic site (residue number reindexed from 1) D157 K159 E161 N162 D175 T192
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:4c35, PDBe:4c35, PDBj:4c35
PDBsum4c35
PubMed24072592
UniProtP00517|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

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