Structure of PDB 2f7e Chain E Binding Site BS02

Receptor Information
>2f7e Chain E (length=336) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHME
TGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNS
NLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIY
RDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKG
YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSD
LKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPF
IPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Ligand information
Ligand ID2EA
InChIInChI=1S/C25H22N4O/c26-22(10-21-14-29-25-4-2-1-3-24(21)25)16-30-23-11-20(13-28-15-23)17-5-6-19-12-27-8-7-18(19)9-17/h1-9,11-15,21-22H,10,16,26H2/t21?,22-/m0/s1
InChIKeyBUCZDJYEOAQTHL-KEKNWZKVSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[C@H](COc1cncc(c1)c2ccc3cnccc3c2)C[C@H]4C=Nc5ccccc45
CACTVS 3.341N[CH](COc1cncc(c1)c2ccc3cnccc3c2)C[CH]4C=Nc5ccccc45
OpenEye OEToolkits 1.5.0c1ccc2c(c1)C(C=N2)C[C@@H](COc3cc(cnc3)c4ccc5cnccc5c4)N
ACDLabs 10.04n2ccc1cc(ccc1c2)c5cc(OCC(N)CC3c4ccccc4N=C3)cnc5
OpenEye OEToolkits 1.5.0c1ccc2c(c1)C(C=N2)CC(COc3cc(cnc3)c4ccc5cnccc5c4)N
FormulaC25 H22 N4 O
Name(1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-3-YL)OXY]METHYL}ETHYLAMINE
ChEMBL
DrugBankDB06959
ZINC
PDB chain2f7e Chain E Residue 351 [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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PDB2f7e Synthesis and structure-activity relationship of 3,4'-bispyridinylethylenes: discovery of a potent 3-isoquinolinylpyridine inhibitor of protein kinase B (PKB/Akt) for the treatment of cancer.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		T51 G52 R56 A70 K72 Y122 V123 N171 L173 T183 D184 F327
Binding residue
(residue number reindexed from 1)		T37 G38 R42 A56 K58 Y108 V109 N157 L159 T169 D170 F313
Annotation score1
Binding affinityMOAD: ic50=1.3nM
Enzymatic activity
Catalytic site (original residue number in PDB) N171 D184
Catalytic site (residue number reindexed from 1) N157 D170
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:2f7e, PDBe:2f7e, PDBj:2f7e
PDBsum2f7e
PubMed16413780
UniProtP00517|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

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