MolNFT v1 · #13389 · protein
Structure of gamma-glutamyl hydrolase
1L9X: “Structure of gamma-glutamyl hydrolase”. X-ray diffraction, 18 pockets (best druggability 0.75). MolNFT v1 #13389 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1L9X
- Type
- protein
- Length
- 1,163 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyl hydrolase
- EC
- 3.4.19.9
- UniProt
- Q92820
- Pockets
- 18 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Gamma-glutamyl hydrolase (EC 3.4.19.9) | protein | 288 | 36% helix, 25% strand | Q92820 |
| B | Gamma-glutamyl hydrolase (EC 3.4.19.9) | protein | 294 | 35% helix, 25% strand | Q92820 |
| D | Gamma-glutamyl hydrolase (EC 3.4.19.9) | protein | 293 | 36% helix, 25% strand | Q92820 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.75 | 0.97 | 25 | empty |
| 2 | 76 | 0.73 | 0.97 | 26 | empty |
| 3 | 814 | 0.73 | 0.78 | 76 | empty |
| 4 | 311 | 0.60 | 0.78 | 39 | BME |
| 5 | 251 | 0.57 | 0.78 | 33 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1526 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1525 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 475 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 347 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 6 covalent (additive adduct).
Compared structures
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 Q92820
- Elsewhere: RCSB PDB 1L9X · PDBe 1L9X · UniProt Q92820
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