Structure of PDB 3mvh Chain A

Receptor sequence
>3mvhA (length=312) Species: 9606 (Homo sapiens) [Search protein sequence]
VTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAH
TLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERV
FSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFG
LCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGG
GSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTA
QRPHFPQFDYSA
3D structure
PDB3mvh Design of selective, ATP-competitive inhibitors of Akt.
ChainA
Resolution2.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D274 K276 N279 D292 T312
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 H194 E234 F236 D274 K276 E278 F309 C310 G311 T312 P313 E314 Y315 E341 H50 E90 F92 D130 K132 E134 F165 C166 G167 T168 P169 E170 Y171 E197
BS02 MN A E314 H354 E170 H210
BS03 WFE A L156 G157 K158 G162 V164 A177 M227 E228 Y229 A230 E234 M281 T291 D292 F438 L12 G13 K14 G18 V20 A33 M83 E84 Y85 A86 E90 M137 T147 D148 F294 MOAD: ic50=0.5nM
PDBbind-CN: -logKd/Ki=9.30,IC50=0.5nM
BindingDB: IC50=0.5nM
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:3mvh, PDBe:3mvh, PDBj:3mvh
PDBsum3mvh
PubMed20481595
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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