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Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor C-met in complex with a pyrrolopyridinepyridone based inhibitor

Analyse Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CE3
Type: protein
Length: 293 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: 1FN
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatocyte growth factor receptor (EC 2.7.10.1)	protein	293	34% helix, 10% strand	P08581

Ligands and binding sites

1FN · 1-(4-fluorophenyl)-N-[3-fluoro-4-(1H-pyrrolo[2,3-b]pyridin-4-yloxy)phenyl]-2-oxo-1,2-dihydropyridine-3-carboxamide · ligand · chains A

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

Pockets

2 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	635	0.77	0.82	74	1FN
2	55	0.29	0.75	15	empty

Compared structures

3CE3 · Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor… · 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 3CE3 · PDBe 3CE3 · UniProt P08581

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