MolNFT v1 · #70634 · protein

Structure of the kinase domain of C-met bound to XL880 (GSK1363089)

3LQ8 · Hepatocyte growth factor receptor: “Structure of the kinase domain of C-met bound to XL880 (GSK1363089)”. X-ray diffraction, 1 ligand (88Z), 1 pocket (best druggability 0.74). MolNFT v1 #70634 on GenesisL1: 3D structure, binding…

PDB: 3LQ8
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hepatocyte growth factor receptor
EC: 2.7.10.1
UniProt: P08581
Ligands: 88Z
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatocyte growth factor receptor (EC 2.7.10.1)	protein	278	44% helix, 17% strand	P08581

Ligands and binding sites

88Z · N-(3-fluoro-4-{[6-methoxy-7-(3-morpholin-4-ylpropoxy) quinolin-4-yl]oxy}phenyl)-N'-(4-fluorophenyl) cyclopropane-1,1-dicarboxamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	579	0.74	0.81	59	88Z

Compared structures

3LQ8 · Structure of the kinase domain of c-Met bound to XL880 (GSK1363089) · 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 P08581
Elsewhere: RCSB PDB 3LQ8 · PDBe 3LQ8 · UniProt P08581

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