Structure of PDB 3zo1 Chain A Binding Site BS02

Receptor Information
>3zo1 Chain A (length=342) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVM
LVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEF
SFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLH
SLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPE
IILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFP
SHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQR
KVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Ligand information
Ligand IDSIJ
InChIInChI=1S/C14H20N6/c1-2-6-19-14(3-1)4-7-20(8-5-14)13-11-12(16-9-15-11)17-10-18-13/h9-10,19H,1-8H2,(H,15,16,17,18)
InChIKeySLPPJSSITOXUMX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01n4c1c(ncnc1N3CCC2(NCCCC2)CC3)nc4
CACTVS 3.385C1CCC2(CCN(CC2)c3ncnc4[nH]cnc34)NC1
OpenEye OEToolkits 1.9.2c1[nH]c2c(n1)c(ncn2)N3CCC4(CCCCN4)CC3
FormulaC14 H20 N6
Name6-(1,9-DIAZASPIRO[5.5]UNDECAN-9-YL)-9H-PURINE
ChEMBLCHEMBL2420909
DrugBank
ZINCZINC000095920627
PDB chain3zo1 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

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3zo1 Synthesis and evaluation of heteroaryl substituted diazaspirocycles as scaffolds to probe the ATP-binding site of protein kinases.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		V57 A70 V104 M120 E121 Y122 V123 E127 E170 L173 D184 F327
Binding residue
(residue number reindexed from 1)		V49 A62 V96 M112 E113 Y114 V115 E119 E162 L165 D176 F319
Annotation score1
Binding affinityMOAD: ic50=1uM
PDBbind-CN: -logKd/Ki=6.00,IC50=1uM
Enzymatic activity
Catalytic site (original residue number in PDB) D166 K168 E170 N171 D184 T201
Catalytic site (residue number reindexed from 1) D158 K160 E162 N163 D176 T193
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3zo1, PDBe:3zo1, PDBj:3zo1
PDBsum3zo1
PubMed23920481
UniProtP00517|KAPCA_BOVIN cAMP-dependent protein kinase catalytic subunit alpha (Gene Name=PRKACA)

[Back to BioLiP]