MolNFT v1 · #121368 · protein
Crystal structure of C-met kinase domain in complex with LXM108
5HTI · Hepatocyte growth factor receptor: “Crystal structure of C-met kinase domain in complex with LXM108”. X-ray diffraction, 1 ligand (66L), 1 pocket (best druggability 0.75). MolNFT v1 #121368 on GenesisL1: 3D structure, binding sites…
- PDB
- 5HTI
- Type
- protein
- Length
- 290 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
- 66L
- Pockets
- 1 · best druggability 0.75
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 | 290 | 41% helix, 17% strand | P08581 |
Ligands and binding sites
- 66L · N-[3-fluoro-4-({7-[2-(morpholin-4-yl)ethoxy]-1,6-naphthyridin-4-yl}oxy)phenyl]-N'-(4-fluorophenyl)cyclopropane-1,1-dicarboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 468 | 0.75 | 0.83 | 53 | 66L |
Compared structures
- 5HTI · Crystal structure of c-Met kinase domain in complex with LXM108 · 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 5HTI · PDBe 5HTI · UniProt P08581
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