Research workbench
Human glutathione transferase O1-1 C32S mutant in complex with ascorbic acid
Analyse Human glutathione transferase O1-1 C32S mutant in complex with ascorbic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VLN
- Type
- protein
- Length
- 239 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
- UniProt
- P78417
- Ligands
- ASC, SO4
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase omega-1 (EC 2.5.1.18) | protein | 239 | 53% helix, 8% strand | P78417 |
Ligands and binding sites
- ASC · Ascorbic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 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 | 168 | 0.53 | 0.78 | 22 | ASC, ACT |
| 2 | 75 | 0.29 | 0.72 | 15 | SO4, GOL |
Compared structures
- 3VLN · Human Glutathione Transferase O1-1 C32S Mutant in Complex with Ascorbic Acid · the same entry in another collection · chain A against A, TM-score 1.00
- P78417 · AlphaFold monomer V2.0 prediction for glutathione S-transferase omega-1 (P78417) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 3VLN · PDBe 3VLN · UniProt P78417
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