Structure of PDB 2bmc Chain B

Receptor sequence
>2bmcB (length=258) Species: 9606 (Homo sapiens) [Search protein sequence]
KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGV
EHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQK
LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIAD
FGWSVTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQE
TYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITAN
SSKPSNCQ
3D structure
PDB2bmc Potent and Selective Aurora Inhibitors Identified by the Expansion of a Novel Scaffold for Protein Kinase Inhibition.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D256 K258 E260 N261 D274 T292
Catalytic site (residue number reindexed from 1) D132 K134 E136 N137 D150 T156
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 MPY B G140 K141 V147 K162 Y212 A213 P214 G216 L263 G16 K17 V23 K38 Y88 A89 P90 G92 L139
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0000212 meiotic spindle organization
GO:0000226 microtubule cytoskeleton organization
GO:0000278 mitotic cell cycle
GO:0006468 protein phosphorylation
GO:0007052 mitotic spindle organization
GO:0007098 centrosome cycle
GO:0007100 mitotic centrosome separation
GO:0051321 meiotic cell cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:2bmc, PDBe:2bmc, PDBj:2bmc
PDBsum2bmc
PubMed15828847
UniProtO14965|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA)

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