MolNFT v1 · #92688 · protein
Crystal structure of cmet in complex with novel inhibitor
4GG5 · Hepatocyte growth factor receptor: “Crystal structure of cmet in complex with novel inhibitor”. X-ray diffraction, 1 ligand (0J3), 3 pockets (best druggability 0.66). MolNFT v1 #92688 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4GG5
- Type
- protein
- Length
- 274 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
- 0J3
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 274 | 38% helix, 19% strand | P08581 |
Ligands and binding sites
- 0J3 · 3-(4-methylpiperazin-1-yl)-N-(3-nitrobenzyl)-7-(trifluoromethyl)quinolin-5-amine · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.66 | 0.84 | 25 | 0J3 |
| 2 | 132 | 0.46 | 0.77 | 23 | empty |
| 3 | 75 | 0.40 | 0.78 | 16 | empty |
Compared structures
- 4GG5 · 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 4GG5 · PDBe 4GG5 · UniProt P08581
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