Research workbench
First-sphere and second-sphere electrostatic effects in the active site of a class mu glutathione transferase
Analyse First-sphere and second-sphere electrostatic effects in the active site of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GSX
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04905
- Ligands
- GPS, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 217 | — | P04905 |
Ligands and binding sites
- GPS · L-gamma-glutamyl-S-[(9S,10S)-10-hydroxy-9,10-dihydrophenanthren-9-yl]-L-cysteinylglycine · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GSX · First-sphere and second-sphere electrostatic effects in the active site of a class mu… · 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 6GSX · PDBe 6GSX · UniProt P04905
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