MolNFT v1 · #118321 · protein

Crystal structure of C-met in complex with amg 337

5EYD · Hepatocyte growth factor receptor: “Crystal structure of C-met in complex with amg 337”. X-ray diffraction, 1 ligand (5T1), 3 pockets (best druggability 0.63). MolNFT v1 #118321 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5EYD
Type: protein
Length: 289 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: 5T1
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatocyte growth factor receptor (EC 2.7.10.1)	protein	289	43% helix, 15% strand	P08581

Ligands and binding sites

5T1 · 6-[(1~{R})-1-[8-fluoranyl-6-(1-methylpyrazol-4-yl)-[1,2,4]triazolo[4,3-a]pyridin-3-yl]ethyl]-3-(2-methoxyethoxy)-1,6-naphthyridin-5-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	204	0.63	0.83	26	5T1
2	96	0.39	0.76	13	empty
3	89	0.38	0.76	14	empty

Compared structures

5EYD · Crystal structure of c-Met in complex with AMG 337 · 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 5EYD · PDBe 5EYD · UniProt P08581

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