BioLiP

Structure of PDB 2jdo Chain A

Receptor sequence

>2jdoA (length=315) Species: 9606 (Homo sapiens) [Search protein sequence]

KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITMFEDFDYIADW

3D structure

PDB

2jdo A Structural Comparison of Inhibitor Binding to Pkb, Pka and Pka-Pkb Chimera

Chain

Resolution

1.8 Å

3D
structure

Catalytic site residues are labeled in the structure
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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	E236 F238 D275 K277 E279 F310 C311 G312 T313 P314 E315 Y316 E342 L348	E91 F93 D130 K132 E134 F165 C166 G167 T168 P169 E170 Y171 E197 L203
BS02	I5S	A	G159 K160 G161 G164 K165 V166 A179 K181 M229 A232 E279 N280 M282 D293	G14 K15 G16 G19 K20 V21 A34 K36 M84 A87 E134 N135 M137 D148	MOAD: ic50=0.23uM PDBbind-CN: -logKd/Ki=6.64,IC50=0.23uM BindingDB: IC50=260nM

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

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:2jdo, PDBe:2jdo, PDBj:2jdo
PDBsum	2jdo
PubMed	17275837
UniProt	P31751\|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)