Research workbench
Ligand-free human glutathione S-transferase M1A-1A
Analyse Ligand-free human glutathione S-transferase M1A-1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GTU
- Type
- protein
- Length
- 868 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- P09488
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glutathione S-transferase (EC 2.5.1.18) | protein | 217 | 52% helix, 10% strand | P09488 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 997 | 0.78 | 0.80 | 78 | empty |
| 2 | 970 | 0.77 | 0.80 | 78 | empty |
| 3 | 215 | 0.66 | 0.84 | 21 | empty |
| 4 | 229 | 0.65 | 0.84 | 26 | empty |
| 5 | 399 | 0.59 | 0.75 | 44 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1448 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1437 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 404 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P09488
- Elsewhere: RCSB PDB 1GTU · PDBe 1GTU · UniProt P09488
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