Structure of PDB 2wtv Chain D

Receptor sequence
>2wtvD (length=265) Species: 9606 (Homo sapiens) [Search protein sequence]
KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGV
EHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPRGEVYKELQK
LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIAD
FGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV
GKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPML
REVLEHPWITANSSK
3D structure
PDB2wtv Crystal Structure of an Aurora-A Mutant that Mimics Aurora-B Bound to Mln8054: Insights Into Selectivity and Drug Design.
ChainD
Resolution2.4 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 T168
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 ZZL D G140 K141 V147 L194 Y212 A213 G216 L263 A273 D274 G276 V279 G16 K17 V23 L70 Y88 A89 G92 L139 A149 D150 G152 V155 MOAD: Ki=1.8nM
BindingDB: IC50=34nM,Kd=6.5nM
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:2wtv, PDBe:2wtv, PDBj:2wtv
PDBsum2wtv
PubMed20067443
UniProtO14965|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA)

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