Research workbench
Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor C-met
Analyse Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R1W
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte growth factor receptor
- EC
- 2.7.1.112
- UniProt
- P08581
- Pockets
- 3 · 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 2.7.1.112) | protein | 287 | 41% helix, 17% strand | P08581 |
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 | 152 | 0.60 | 0.83 | 22 | empty |
| 2 | 85 | 0.37 | 0.76 | 22 | empty |
| 3 | 63 | 0.29 | 0.74 | 15 | empty |
Compared structures
- 1R1W · Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor… · 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 0.87
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 1R1W · PDBe 1R1W · UniProt P08581
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.