Structure of PDB 3ocb Chain B

Receptor sequence
>3ocbB (length=320) Species: 9606 (Homo sapiens) [Search protein sequence]
RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRER
VFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDF
GLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM
CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG
GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT
AQMITITRPHFPQFDYSASS
3D structure
PDB3ocb Discovery of pyrrolopyrimidine inhibitors of Akt.
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) 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 B E234 F236 D274 K276 L277 E278 F309 C310 G311 T312 P313 E314 Y315 L316 E341 L347 E91 F93 D131 K133 L134 E135 F166 C167 G168 T169 P170 E171 Y172 L173 E198 L204
BS02 XM1 B G159 G162 A177 K179 M227 E278 N279 M281 T291 D292 F438 G16 G19 A34 K36 M84 E135 N136 M138 T148 D149 F295 BindingDB: IC50=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:3ocb, PDBe:3ocb, PDBj:3ocb
PDBsum3ocb
PubMed20810279
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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