MolNFT v1 · #60750 · protein

Crystal structure of mouse aurora a (ASN186->gly, LYS240->arg, MET302- >leu) in complex with 1-{5-[2-(THIENO[3,2-D]PYRIMIDIN-4-ylamino)- ethyl]- thiazol-2-yl}-3-(3-trifluoromethyl-phenyl)-urea

3D14 · SERINE/THREONINE kinase 6: “Crystal structure of mouse aurora a (ASN186->gly, LYS240->arg, MET302- >leu) in complex with…”. X-ray diffraction, 1 ligand (AK1), 3 pockets (best druggability 0.75). MolNFT v1 #60750 on GenesisL1: 3D…

PDB: 3D14
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE kinase 6
EC: 2.7.11.1
UniProt: Q8C3H8
Ligands: AK1
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE kinase 6 (EC 2.7.11.1)	protein	262	42% helix, 18% strand	Q8C3H8

Ligands and binding sites

AK1 · 1-{5-[2-(thieno[3,2-d]pyrimidin-4-ylamino)ethyl]-1,3-thiazol-2-yl}-3-[3-(trifluoromethyl)phenyl]urea · ligand · 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	399	0.75	0.84	42	AK1
2	60	0.34	0.77	14	empty
3	57	0.29	0.74	15	empty

Compared structures

3D14 · Crystal structure of mouse Aurora A (Asn186->Gly, Lys240->Arg, Met302->Leu) in complex… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q8C3H8
Elsewhere: RCSB PDB 3D14 · PDBe 3D14 · UniProt Q8C3H8

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