Structure of PDB 6vpl Chain B

Receptor sequence
>6vplB (length=277) Species: 9606 (Homo sapiens) [Search protein sequence]
MSYSYDAPSDFINFSSKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFI
LALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYL
ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIK
PENLLLGSAGELKIADFGWSVHAPTTLCGTLDYLPPEMIEGRMHDEKVDL
WSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISR
LLKHNPSQRPMLREVLEHPWITANSSK
3D structure
PDB6vpl Redox priming promotes Aurora A activation during mitosis.
ChainB
Resolution1.86 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) D148 K150 E152 N153 D166 T180
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 MG B S7 E175 H176 S2 E67 H68
BS02 R7D B W277 M305 Y338 W169 M193 Y226
BS03 ANP B G142 K143 F144 A160 K162 E211 A213 G34 K35 F36 A52 K54 E103 A105
BS04 MG B K162 E181 K54 E73
BS05 R7D B L289 C290 M300 I301 L177 C178 M188 I189
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:6vpl, PDBe:6vpl, PDBj:6vpl
PDBsum6vpl
PubMed32694171
UniProtO14965|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA);
Q9ULW0

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