Structure of PDB 2vrx Chain B

Receptor sequence
>2vrxB (length=275) Species: 8355 (Xenopus laevis) [Search protein sequence]
NTALAEMPKRKFTIDDFDIGRPLGGNVYLAREKQNKFIMALKVLFKSQLE
KEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYK
ELQKHGRFDEQRSATFMEELADALHYCHERKVIHRDIKPENLLMGYKGEL
KIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCY
EFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQ
RLPLKGVMEHPWVKANSRRVLPPVY
3D structure
PDB2vrx Molecular Basis of Drug Resistance in Aurora Kinases.
ChainB
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) D136 K138 E140 N141 D154 T172
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 B L99 V107 K122 E141 Q145 L154 L170 F172 A173 G176 E177 L223 A233 F235 L23 V27 K42 E61 Q65 L74 L90 F92 A93 G96 E97 L143 A153 F155 BindingDB: IC50=45nM
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
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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