Research workbench
Human C-met kinase domain complexed with 6-benzyloxyquinoline inhibitor
Analyse Human C-met kinase domain complexed with 6-benzyloxyquinoline inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A4P
- Type
- protein
- Length
- 285 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
- DFQ, CL
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 285 | 38% helix, 18% strand | P08581 |
Ligands and binding sites
- DFQ · (2E)-3-{6-[(1R)-1-(2,6-dichloro-3-fluorophenyl)ethoxy]quinolin-3-yl}-N-methylprop-2-enamide · ligand · chains A
- CL · Chloride ion · ion · chains A
- IPA · Isopropyl alcohol · additive · 2 copies · 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 | 240 | 0.68 | 0.84 | 27 | IPA, DFQ |
| 2 | 187 | 0.50 | 0.77 | 21 | empty |
| 3 | 78 | 0.35 | 0.75 | 19 | empty |
Compared structures
- 3A4P · human c-MET kinase domain complexed with 6-benzyloxyquinoline inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P08581 · AlphaFold monomer V2.0 prediction for hepatocyte growth factor receptor (P08581) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 3A4P · PDBe 3A4P · UniProt P08581
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.