Research workbench
Crystal structure of cmet in complex with a novel inhibitor
Analyse Crystal structure of cmet in complex with a novel inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V3R
- 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
- 5IE
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 285 | 41% helix, 16% strand | P08581 |
Ligands and binding sites
- 5IE · ~{N}1'-[3-fluoranyl-4-(2-phenylazanylpyrimidin-4-yl) oxy-phenyl]-~{N}1-(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
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 | 430 | 0.74 | 0.84 | 52 | 5IE |
| 2 | 50 | 0.32 | 0.78 | 15 | empty |
Compared structures
- 7V3R · Crystal structure of CMET in complex with a 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 7V3R · PDBe 7V3R · UniProt P08581
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