Research workbench
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the mu and pi class enzymes
Analyse Structure determination and refinement of human alpha class glutathione… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GUH
- Type
- protein
- Length
- 884 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P08263
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 221 | — | P08263 |
Compared structures
- 1GUH · Structure determination and refinement of human alpha class glutathione transferase A1-1… · the same entry in another collection · chain A against A, TM-score 1.00
- P08263 · AlphaFold monomer V2.0 prediction for glutathione S-transferase A1 (P08263) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P08263
- Elsewhere: RCSB PDB 1GUH · PDBe 1GUH · UniProt P08263
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.