Structure of PDB 3e5a Chain A

Receptor sequence
>3e5aA (length=265) Species: 9606 (Homo sapiens) [Search protein sequence]
KRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGV
EHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQK
LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIAD
FGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV
GKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPML
REVLEHPWITANSSK
3D structure
PDB3e5a Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2.
ChainA
Resolution2.3 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 VX6 A L139 F144 A160 E211 Y212 A213 P214 G216 T217 L263 A273 D274 L15 F20 A36 E87 Y88 A89 P90 G92 T93 L139 A149 D150 MOAD: Ki=5.9nM
PDBbind-CN: -logKd/Ki=8.23,Ki=5.9nM
BindingDB: Ki=0.600000nM,IC50=20nM,Kd=4.1nM
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:3e5a, PDBe:3e5a, PDBj:3e5a
PDBsum3e5a
PubMed18662907
UniProtO14965|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA)

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