MolNFT v1 · #117978 · protein
Crystal structure of cmet in complex with novel inhibitor
5EOB · Hepatocyte growth factor receptor: “Crystal structure of cmet in complex with novel inhibitor”. X-ray diffraction, 1 ligand (5QQ), 2 pockets (best druggability 0.65). MolNFT v1 #117978 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5EOB
- Type
- protein
- Length
- 288 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
- 5QQ
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 288 | 43% helix, 17% strand | P08581 |
Ligands and binding sites
- 5QQ · 6-[bis(fluoranyl)-[6-(4-fluorophenyl)-[1,2,4]triazolo[4,3-b][1,2,4]triazin-3-yl]methyl]quinoline · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.65 | 0.84 | 26 | 5QQ |
| 2 | 204 | 0.51 | 0.77 | 22 | empty |
Compared structures
- 5EOB · Crystal structure of CMET in complex with novel 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 5EOB · PDBe 5EOB · UniProt P08581
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.