Structure of PDB 3e87 Chain B

Receptor sequence
>3e87B (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITITPPQRTHFPQFDYSASIR
3D structure
PDB3e87 Aminofurazans as potent inhibitors of AKT kinase
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 peptide B E236 F238 D275 K277 L278 E279 F310 C311 G312 T313 P314 L348 E91 F93 D130 K132 L133 E134 F165 C166 G167 T168 P169 L203
BS02 G95 B L158 G164 V166 A179 K181 L183 A232 E279 M282 T292 D293 F439 L13 G19 V21 A34 K36 L38 A87 E134 M137 T147 D148 F294
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3e87, PDBe:3e87, PDBj:3e87
PDBsum3e87
PubMed19179070
UniProtP31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)

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