Structure of PDB 2bfy Chain A

Receptor sequence
>2bfyA (length=271) Species: 8355 (Xenopus laevis) [Search protein sequence]
RKFTIDDFDIVRPLGKGKFGNVYLAREKQNKFIMALKVLFKSQLEKEGVE
HQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKH
GRFDEQRSATFMEELADALHYCHERKVIHRDIKPENLLMGYKGELKIADF
GWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCYEFLVG
MPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLK
GVMEHPWVKANSRRVLPPVYQ
3D structure
PDB2bfy Mechanism of Aurora B Activation by Incenp and Inhibition by Hesperadin
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D216 K218 E220 N221 D234 T252
Catalytic site (residue number reindexed from 1) D131 K133 E135 N136 D149 T167
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 H1N A L99 G100 G102 K103 V107 A120 K122 L154 F172 A173 P174 R175 G176 E177 L223 A233 L14 G15 G17 K18 V22 A35 K37 L69 F87 A88 P89 R90 G91 E92 L138 A148 BindingDB: IC50=3nM
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:2bfy, PDBe:2bfy, PDBj:2bfy
PDBsum2bfy
PubMed15866179
UniProtQ6DE08|AUKBA_XENLA Aurora kinase B-A (Gene Name=aurkb-a)

[Back to BioLiP]