Structure of PDB 2gni Chain A Binding Site BS02

Receptor Information
>2gni 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]
SEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTIGTGSFGRVML
VKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFS
FKDNSNLYMVMEYMPGGDMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS
LDLIYRDLKPENLLIDQQGYIKVADFGFAKRVKGRTWTLCGTPEYLAPEI
ILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPS
HFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRK
VEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Ligand information
Ligand IDM77
InChIInChI=1S/C14H17N3O2S/c18-20(19,17-9-2-6-15-8-10-17)14-4-1-3-12-11-16-7-5-13(12)14/h1,3-5,7,11,15H,2,6,8-10H2
InChIKeyNGOGFTYYXHNFQH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=S(=O)(c2c1ccncc1ccc2)N3CCCNCC3
CACTVS 3.370O=[S](=O)(N1CCCNCC1)c2cccc3cnccc23
OpenEye OEToolkits 1.7.2c1cc2cnccc2c(c1)S(=O)(=O)N3CCCNCC3
FormulaC14 H17 N3 O2 S
Name5-(1,4-DIAZEPAN-1-SULFONYL)ISOQUINOLINE;
Fasudil;
(5-ISOQUINOLINESULFONYL)HOMOPIPERAZINE
ChEMBLCHEMBL38380
DrugBankDB08162
ZINCZINC000000006486
PDB chain2gni Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2gni Structural analysis of protein kinase A mutants with Rho-kinase inhibitor specificity
Resolution2.27 Å
Binding residue
(original residue number in PDB)		I49 V57 A70 M120 Y122 M123 D127 E170 L173 A183 F327
Binding residue
(residue number reindexed from 1)		I40 V48 A61 M111 Y113 M114 D118 E161 L164 A174 F318
Annotation score1
Binding affinityMOAD: ic50=2280nM
PDBbind-CN: -logKd/Ki=5.64,IC50=2.28uM
BindingDB: IC50=1494nM
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:2gni, PDBe:2gni, PDBj:2gni
PDBsum2gni
PubMed16699172
UniProtP00517|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

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