Research workbench
New crystal forms of a mu class glutathione S-transferase from rat liver
Analyse New crystal forms of a mu class glutathione S-transferase from rat liver in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GSC
- Type
- protein
- Length
- 868 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- P04905
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glutathione S-transferase (EC 2.5.1.18) | protein | 217 | 0% helix, 0% strand | P04905 |
Interfaces
3 interfaces between chains.
- A–B · 64 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 64 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 10 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1GSC · New crystal forms of a mu class glutathione S-transferase from rat liver · the same entry in another collection · chain A against A, TM-score 1.00
- P04905 · AlphaFold monomer V2.0 prediction for glutathione S-transferase mu 1 (P04905) · 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 P04905
- Elsewhere: RCSB PDB 1GSC · PDBe 1GSC · UniProt P04905
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