Structure of PDB 2vrx Chain A

Receptor sequence
>2vrxA (length=269) Species: 8355 (Xenopus laevis) [Search protein sequence]
KFTIDDFDIGRPLGKGKFGNVYLAREKQNKFIMALKVLFKSQLEKEGVEH
QLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHG
RFDEQRSATFMEELADALHYCHERKVIHRDIKPENLLMGYKGELKIADFG
WSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCYEFLVGM
PPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKG
VMEHPWVKANSRRVLPPVY
3D structure
PDB2vrx Molecular Basis of Drug Resistance in Aurora Kinases.
ChainA
Resolution1.86 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 447 A L99 V107 K122 E141 Q145 L154 L168 L170 F172 A173 P174 G176 L223 L13 V21 K36 E55 Q59 L68 L82 L84 F86 A87 P88 G90 L137 PDBbind-CN: -logKd/Ki=7.35,IC50=45nM
BindingDB: IC50=45nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vrx, PDBe:2vrx, PDBj:2vrx
PDBsum2vrx
PubMed18559266
UniProtQ6DE08|AUKBA_XENLA Aurora kinase B-A (Gene Name=aurkb-a)

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