MolNFT v1 · #82745 · protein
Crystal structure of human C-met kinase domain with its inhibitor
3VW8 · Hepatocyte growth factor receptor: “Crystal structure of human C-met kinase domain with its inhibitor”. X-ray diffraction, 2 ligands (DF6, CL), 2 pockets (best druggability 0.73). MolNFT v1 #82745 on GenesisL1: 3D structure, binding…
- PDB
- 3VW8
- Type
- protein
- Length
- 303 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
- DF6, CL
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 303 | 39% helix, 16% strand | P08581 |
Ligands and binding sites
- DF6 · N-({4-[(6,7-dimethoxyquinolin-4-yl)oxy]phenyl}carbamothioyl)-2-phenylacetamide · ligand · chains A
- CL · Chloride ion · ion · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.73 | 0.83 | 58 | DF6 |
| 2 | 120 | 0.43 | 0.77 | 15 | empty |
Compared structures
- 3VW8 · Crystal structure of human c-Met kinase domain with its inhibitor · 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 3VW8 · PDBe 3VW8 · UniProt P08581
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