Structure of PDB 3mv5 Chain A

Receptor sequence
>3mv5A (length=316) Species: 9606 (Homo sapiens) [Search protein sequence]
RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRER
VFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDF
GLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM
CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG
GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT
AQMIRPHFPQFDYSAS
3D structure
PDB3mv5 Design of selective, ATP-competitive inhibitors of Akt.
ChainA
Resolution2.47 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) D131 K133 N136 D149 T169
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 E234 F236 D274 K276 E278 F309 C310 G311 T312 E314 Y315 E91 F93 D131 K133 E135 F166 C167 G168 T169 E171 Y172
BS02 MN A E314 H354 E171 H211
BS03 XFE A A177 M227 A230 E234 M281 T291 F438 A34 M84 A87 E91 M138 T148 F295 MOAD: ic50=180nM
PDBbind-CN: -logKd/Ki=6.74,IC50=180nM
BindingDB: IC50=180nM
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:3mv5, PDBe:3mv5, PDBj:3mv5
PDBsum3mv5
PubMed20481595
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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