Structure of PDB 1o6k Chain A

Receptor sequence

>1o6kA (length=318) Species: 9606 (Homo sapiens)

KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITQRTHFPQFDYSASI

3D structure

• PDB: 1o6k Crystal Structure of an Activated Akt/Protein Kinase B Ternary Complex with Gsk-3 Peptide and AMP-Pnp
• Chain: A
• Resolution: 1.7 Å

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	A	T162 E236 F238 K277 E279 F310 C311 G312 T313 P314 E315 Y316 L317 E342 Y351 F443	T17 E91 F93 K132 E134 F165 C166 G167 T168 P169 E170 Y171 L172 E197 Y206 F298
BS02	ANP	A	V166 A179 K181 M229 A232 E236 K277 E279 M282 T292 D293 F439	V21 A34 K36 M84 A87 E91 K132 E134 M137 T147 D148 F294
BS03	MN	A	N280 D293	N135 D148

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

External links

• PDB: RCSB:1o6k, PDBe:1o6k, PDBj:1o6k
• PDBsum: 1o6k
• PubMed: 12434148
• UniProt: P31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)