MolNFT v1 · #90288 · protein
Crystal structure of C-met in complex with LY2801653
4EEV · Hepatocyte growth factor receptor: “Crystal structure of C-met in complex with LY2801653”. X-ray diffraction, 1 ligand (L1X), 2 pockets (best druggability 0.67). MolNFT v1 #90288 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4EEV
- Type
- protein
- Length
- 283 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
- L1X
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 283 | 42% helix, 16% strand | P08581 |
Ligands and binding sites
- L1X · N-(3-fluoro-4-{[1-methyl-6-(1H-pyrazol-4-yl)-1H-indazol-5-yl]oxy}phenyl)-1-(4-fluorophenyl)-6-methyl-2-oxo-1,2-dihydropyridine-3-carboxamide · 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 | 391 | 0.67 | 0.80 | 43 | L1X |
| 2 | 57 | 0.29 | 0.74 | 19 | empty |
Compared structures
- 4EEV · Crystal structure of c-Met in complex with LY2801653 · 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 4EEV · PDBe 4EEV · UniProt P08581
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