Structure of PDB 2bmc Chain D

Receptor sequence
>2bmcD (length=256) Species: 9606 (Homo sapiens) [Search protein sequence]
QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEH
QLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLS
KFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG
WSVTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETY
KRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSS
KPSNCQ
3D structure
PDB2bmc Potent and Selective Aurora Inhibitors Identified by the Expansion of a Novel Scaffold for Protein Kinase Inhibition.
ChainD
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) D130 K132 E134 N135 D148 T154
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 D G140 V147 A160 K162 E211 Y212 A213 P214 G216 L263 G14 V21 A34 K36 E85 Y86 A87 P88 G90 L137
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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