Research workbench
Crystal structure of human microsomal glutathione S-transferase 2 in complex with an inhibitor glutathione sulfonic acid
Analyse Crystal structure of human microsomal glutathione S-transferase 2 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SSW
- Type
- protein
- Length
- 406 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q99735
- Ligands
- GTS
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 136 | — | Q99735 |
| B | — | protein | 140 | — | Q99735 |
| C | — | protein | 130 | — | Q99735 |
Ligands and binding sites
- GTS · Glutathione sulfonic acid · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6SSW · Crystal structure of Human Microsomal Glutathione S-Transferase 2 in complex with an… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99735 · AlphaFold monomer V2.0 prediction for microsomal glutathione S-transferase 2 (Q99735) · a predicted model of the same protein · chain C 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 Q99735
- Elsewhere: RCSB PDB 6SSW · PDBe 6SSW · UniProt Q99735
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