BioLiP

Structure of PDB 4c3r Chain A

Receptor sequence

>4c3rA (length=252) Species: 9606 (Homo sapiens) [Search protein sequence]

QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEH
QLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLS
KFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG
WSVHGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQE
TYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITAN
SS

3D structure

PDB

4c3r Molecular Mechanism of Aurora a Kinase Autophosphorylation and its Allosteric Activation by Tpx2.

Chain

Resolution

2.79 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)	D130 K132 E134 N135 D148 T156
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	ACP	A	K141 G142 V147 A160 K162 A213 T217 N261 L263	K15 G16 V21 A34 K36 A87 T91 N135 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

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:4c3r, PDBe:4c3r, PDBj:4c3r
PDBsum	4c3r
PubMed	24867643
UniProt	O14965\|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA)