Research workbench
Crystal structure of the 26 kda glutathione S-transferase Y7F mutant from schistosoma japonicum complexed with glutathione
Analyse Crystal structure of the 26 kda glutathione S-transferase Y7F mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U87
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase 26 kda
- EC
- 2.5.1.18
- UniProt
- P08515
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase 26 kda (EC 2.5.1.18) | protein | 209 | 53% helix, 8% strand | P08515 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.50 | 0.81 | 25 | empty |
| 2 | 120 | 0.47 | 0.78 | 15 | empty |
| 3 | 52 | 0.28 | 0.74 | 12 | empty |
Compared structures
- 1U87 · Crystal Structure Of The 26 Kda Glutathione S-Transferase Y7F mutant From Schistosoma… · the same entry in another collection · chain A against A, TM-score 1.00
- P08515 · AlphaFold monomer V2.0 prediction for glutathione S-transferase class-mu 26 kda isozyme… · 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 P08515
- Elsewhere: RCSB PDB 1U87 · PDBe 1U87 · UniProt P08515
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