Structure of PDB 3d0e Chain B

Receptor sequence
>3d0eB (length=324) Species: 9606 (Homo sapiens) [Search protein sequence]
KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITITPPDQRTHFPQFDYSASIR
3D structure
PDB3d0e Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D275 K277 N280 D293 T313
Catalytic site (residue number reindexed from 1) D130 K132 N135 D148 T168
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 G93 B V166 A179 K181 E200 L204 F227 M229 Y231 A232 E236 E279 M282 D293 F294 F439 F443 V21 A34 K36 E55 L59 F82 M84 Y86 A87 E91 E134 M137 D148 F149 F294 F298 MOAD: ic50=13nM
BindingDB: IC50=13nM,Kd=2.1nM,Ki=4nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3d0e, PDBe:3d0e, PDBj:3d0e
PDBsum3d0e
PubMed18800763
UniProtP31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)

[Back to BioLiP]