Structure of PDB 3e8d Chain B

Receptor sequence
>3e8dB (length=318) Species: 9606 (Homo sapiens) [Search protein sequence]
KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSIQRTHFPQFDYSASIR
3D structure
PDB3e8d Aminofurazans as potent inhibitors of AKT kinase
ChainB
Resolution2.7 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 E193 E236 F238 D275 K277 E279 F310 C311 G312 T313 P314 E315 L348 E48 E91 F93 D130 K132 E134 F165 C166 G167 T168 P169 E170 L203
BS02 G98 B K160 G164 V166 A179 K181 E200 L204 F227 M229 M282 T292 D293 F439 K15 G19 V21 A34 K36 E55 L59 F82 M84 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
View graph for
Biological Process
External links
PDB RCSB:3e8d, PDBe:3e8d, PDBj:3e8d
PDBsum3e8d
PubMed19179070
UniProtP31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)

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