Structure of PDB 3e87 Chain A

Receptor sequence
>3e87A (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
ChainA
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 A E236 F238 D275 K277 L278 E279 F310 C311 G312 T313 P314 E315 Y316 E342 L348 E91 F93 D130 K132 L133 E134 F165 C166 G167 T168 P169 E170 Y171 E197 L203
BS02 G95 A G164 V166 A179 K181 Y231 A232 M282 T292 D293 F439 G19 V21 A34 K36 Y86 A87 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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