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
PDB2jdo A Structural Comparison of Inhibitor Binding to Pkb, Pka and Pka-Pkb Chimera
ChainA
Resolution1.8 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

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Molecular Function

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Biological Process
External links
PDB RCSB:2jdo, PDBe:2jdo, PDBj:2jdo
PDBsum2jdo
PubMed17275837
UniProtP31751|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)

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