Structure of PDB 3e8d Chain A

Receptor sequence

>3e8dA (length=316) Species: 9606 (Homo sapiens)

KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITHFPQFDYSASIR

3D structure

• PDB: 3e8d Aminofurazans as potent inhibitors of AKT kinase
• Chain: A
• Resolution: 2.7 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	E193 E236 F238 D275 K277 E279 L296 F310 C311 G312 T313 P314 E315 L348 Y351	E48 E91 F93 D130 K132 E134 L151 F165 C166 G167 T168 P169 E170 L203 Y206
BS02	G98	A	K160 G164 V166 A179 K181 E200 L204 F227 M229 M282 T292 D293 F439	K15 G19 V21 A34 K36 E55 L59 F82 M84 M137 T147 D148 F294

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:3e8d, PDBe:3e8d, PDBj:3e8d
• PDBsum: 3e8d
• PubMed: 19179070
• UniProt: P31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)