Structure of PDB 1o6l Chain A

Receptor sequence

>1o6lA (length=317) Species: 9606 (Homo sapiens)

KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITQEMFEDFDYIADW

3D structure

• PDB: 1o6l Crystal Structure of an Activated Akt/Protein Kinase B Ternary Complex with Gsk-3 Peptide and AMP-Pnp
• Chain: A
• Resolution: 1.6 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	E193 E236 F238 K277 E279 F310 C311 G312 T313 P314 E315 Y316 L317 E342	E48 E91 F93 K132 E134 F165 C166 G167 T168 P169 E170 Y171 L172 E197
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:1o6l, PDBe:1o6l, PDBj:1o6l
• PDBsum: 1o6l
• PubMed: 12434148
• UniProt: P31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)