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Aurora a in complex with RK2-17-01

Analyse Aurora a in complex with RK2-17-01 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DEB
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aurora kinase a
EC: 2.7.11.1
UniProt: O14965
Ligands: NHJ
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aurora kinase a (EC 2.7.11.1)	protein	264	39% helix, 18% strand	O14965

Ligands and binding sites

NHJ · 4-[(4-{[3-(trifluoromethyl)phenyl]amino}pyrimidin-2-yl)amino]benzamide · ligand · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	392	0.68	0.81	42	NHJ
2	71	0.32	0.74	12	empty
3	58	0.28	0.74	15	empty

Compared structures

4DEB · Aurora A in complex with RK2-17-01 · the same entry in another collection · chain A against A, TM-score 1.00
O14965 · AlphaFold monomer V2.0 prediction for aurora kinase a (O14965) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O14965
Elsewhere: RCSB PDB 4DEB · PDBe 4DEB · UniProt O14965

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