Structure of PDB 3qkm Chain A

Receptor sequence
>3qkmA (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRER
VFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDF
GLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM
CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG
GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT
AQMITITPSMECVDSERRPHFPQFDYSASS
3D structure
PDB3qkm Discovery of spirocyclic sulfonamides as potent Akt inhibitors with exquisite selectivity against PKA.
ChainA
Resolution2.2 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 SM9 A G157 K158 G159 F161 G162 K163 V164 A177 E191 M227 A230 E234 E278 M281 D292 F438 G14 K15 G16 F18 G19 K20 V21 A34 E48 M84 A87 E91 E135 M138 D149 F295 MOAD: ic50=0.038uM
PDBbind-CN: -logKd/Ki=7.42,IC50=38nM
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:3qkm, PDBe:3qkm, PDBj:3qkm
PDBsum3qkm
PubMed21420856
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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