Research workbench
Crystal structure of C-met in complex with novel inhibitor
Analyse Crystal structure of C-met in complex with novel inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YA5
- Type
- protein
- Length
- 273 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
- 6TD
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 273 | 41% helix, 17% strand | P08581 |
Ligands and binding sites
- 6TD · 2-[3-(4-methoxybenzyl)[1,2,4]triazolo[3,4-B][1,3, 4]thiadiazol-6-yl]-1H-indole · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.60 | 0.81 | 24 | 6TD |
| 2 | 69 | 0.35 | 0.76 | 13 | empty |
Compared structures
- 5YA5 · CRYSTAL STRUCTURE OF c-MET 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 5YA5 · PDBe 5YA5 · UniProt P08581
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