Research workbench
Human glutathione S-transferase M2-2 (E.C.2.5.1.18)COMPLEXED with glutathione, monoclinic crystal form
Analyse Human glutathione S-transferase M2-2 (E.C.2.5.1.18)COMPLEXED with glutathione… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XW5
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase mu 2
- EC
- 2.5.1.18
- UniProt
- P28161
- Ligands
- GSH
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase mu 2 (EC 2.5.1.18) | protein | 217 | 51% helix, 10% strand | P28161 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 903 | 0.76 | 0.79 | 84 | GSH |
| 2 | 104 | 0.43 | 0.78 | 19 | empty |
| 3 | 73 | 0.37 | 0.77 | 11 | empty |
| 4 | 54 | 0.32 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1427 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1XW5 · Human glutathione s-transferase M2-2 (E.C.2.5.1.18)complexed with glutathione, monoclinic… · the same entry in another collection · chain A against A, TM-score 1.00
- P28161 · AlphaFold monomer V2.0 prediction for glutathione S-transferase mu 2 (P28161) · 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 P28161
- Elsewhere: RCSB PDB 1XW5 · PDBe 1XW5 · UniProt P28161
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