Research workbench
1.8 ångströms molecular structure of mouse liver class pi glutathione S-transferase complexed with S-(P-NITROBENZYL)GLUTATHIONE and other inhibitors
Analyse 1.8 ångströms molecular structure of mouse liver class pi glutathione… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GLQ
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19157
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 209 | — | P19157 |
Compared structures
- 1GLQ · 1.8 ångströms molecular structure of mouse liver class pi glutathione S-transferase… · the same entry in another collection · chain A against A, TM-score 1.00
- P19157 · AlphaFold monomer V2.0 prediction for glutathione S-transferase P 1 (P19157) · 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 P19157
- Elsewhere: RCSB PDB 1GLQ · PDBe 1GLQ · UniProt P19157
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