Structure of PDB 6vpm Chain B

Receptor sequence
>6vpmB (length=277) Species: 9606 (Homo sapiens) [Search protein sequence]
MSYSYDAPSDFINFSSKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFI
LALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYL
ILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIK
PENLLLGSAGELKIADFGWSVHAPTTLCGTLDYLPPEMIEGRMHDEKVDL
WSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISR
LLKHNPSQRPMLREVLEHPWITANSSK
3D structure
PDB6vpm Redox priming promotes Aurora A activation during mitosis.
ChainB
Resolution1.58 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 S2 E67
BS02 R74 B M305 Y338 M193 Y226
BS03 AMP B G140 A160 K162 E211 A213 G32 A52 K54 E103 A105
BS04 R74 B C290 M300 I301 H306 C178 M188 I189 H194
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6vpm, PDBe:6vpm, PDBj:6vpm
PDBsum6vpm
PubMed32694171
UniProtO14965|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA);
Q9ULW0

[Back to BioLiP]