Structure of PDB 2vgo Chain A

Receptor sequence
>2vgoA (length=269) Species: 8355 (Xenopus laevis) [Search protein sequence]
KFTIDDFDIGRPLGKGKFGNVYLAREKQNKFIMALKVLFKSQLEKEGVEH
QLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHG
RFDEQRSATFMEELADALHYCHERKVIHRDIKPENLLMGYKGELKIADFG
WSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCYEFLVGM
PPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKG
VMEHPWVKANSRRVLPPVY
3D structure
PDB2vgo Reversine, a Novel Aurora Kinases Inhibitor, Inhibits Colony Formation of Human Acute Myeloid Leukemia Cells.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D216 K218 E220 N221 D234 T252
Catalytic site (residue number reindexed from 1) D130 K132 E134 N135 D148 T166
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 AD5 A G100 V107 A120 L154 L170 E171 F172 A173 G176 E177 L223 G14 V21 A34 L68 L84 E85 F86 A87 G90 E91 L137 MOAD: ic50=500nM
PDBbind-CN: -logKd/Ki=6.30,IC50=500nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:2vgo, PDBe:2vgo, PDBj:2vgo
PDBsum2vgo
PubMed18483302
UniProtQ6DE08|AUKBA_XENLA Aurora kinase B-A (Gene Name=aurkb-a)

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