Research workbench
Crystal structure of gsh-dependent disulfide bond oxidoreductase
Analyse Crystal structure of gsh-dependent disulfide bond oxidoreductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GX0
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GST-like protein yfcg
- UniProt
- P77526
- Ligands
- GDS
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GST-like protein yfcg | protein | 204 | 59% helix, 10% strand | P77526 |
Ligands and binding sites
- GDS · Oxidized glutathione disulfide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.43 | 0.76 | 23 | GDS |
Compared structures
- 3GX0 · Crystal Structure of GSH-dependent Disulfide bond Oxidoreductase · the same entry in another collection · chain A against A, TM-score 1.00
- P77526 · AlphaFold monomer V2.0 prediction for disulfide-bond oxidoreductase yfcg (P77526) · a predicted model of the same protein · 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 P77526
- Elsewhere: RCSB PDB 3GX0 · PDBe 3GX0 · UniProt P77526
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