MolNFT v1 · #141081 · protein
Human glutathione transferase OMEGA1
5YVN · Glutathione S-transferase omega-1: “Human glutathione transferase OMEGA1”. X-ray diffraction, 2 ligands (GSH, SO4), 2 pockets (best druggability 0.57). MolNFT v1 #141081 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5YVN
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase omega-1
- EC
- 2.5.1.18, 1.8.5.1, 1.20.4.2
- UniProt
- P78417
- Ligands
- GSH, SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase omega-1 (EC 2.5.1.18, 1.8.5.1, 1.20.4.2) | protein | 238 | 52% helix, 8% strand | P78417 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- ACT · Acetate ion · additive · 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 | 194 | 0.57 | 0.79 | 24 | GSH |
| 2 | 69 | 0.28 | 0.73 | 18 | SO4 |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 P78417
- Elsewhere: RCSB PDB 5YVN · PDBe 5YVN · UniProt P78417
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