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Crystal structure of C-met in complex with triazolopyridinone inhibitor 3

Analyse Crystal structure of C-met in complex with triazolopyridinone inhibitor 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DEH
Type: protein
Length: 286 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: 0JK
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatocyte growth factor receptor (EC 2.7.10.1)	protein	286	42% helix, 15% strand	P08581

Ligands and binding sites

0JK · 5-phenyl-3-(quinolin-6-ylmethyl)-3,5,6,7-tetrahydro-4H-[1,2,3]triazolo[4,5-c]pyridin-4-one · 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	203	0.61	0.82	26	0JK
2	147	0.46	0.76	21	empty
3	109	0.46	0.79	14	empty

Compared structures

4DEH · Crystal structure of c-Met in complex with triazolopyridi inhibitor 3 · 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 4DEH · PDBe 4DEH · UniProt P08581

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