MolNFT v1 · #163790 · protein
Crystal structure of D1228V cmet bound by bms-777607
6SDD · Hepatocyte growth factor receptor: “Crystal structure of D1228V cmet bound by bms-777607”. X-ray diffraction, 1 ligand (353), 1 pocket (best druggability 0.75). MolNFT v1 #163790 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6SDD
- Type
- protein
- Length
- 271 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
- 353
- Pockets
- 1 · best druggability 0.75
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 | 271 | 39% helix, 16% strand | P08581 |
Ligands and binding sites
- 353 · N-{4-[(2-amino-3-chloropyridin-4-yl)oxy]-3-fluorophenyl}-4-ethoxy-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide · ligand · chains A
- GOL · Glycerol · additive · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 629 | 0.75 | 0.81 | 57 | 353 |
Compared structures
- 6SDD · Crystal structure of D1228V cMET bound by BMS-777607 · 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 6SDD · PDBe 6SDD · UniProt P08581
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