Research workbench
Crystal structure analysis of apo glutathione S-transferase
Analyse Crystal structure analysis of apo glutathione S-transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K3O
- Type
- protein
- Length
- 406 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase A1
- EC
- 2.5.1.18
- UniProt
- P08263
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase A1 (EC 2.5.1.18) | protein | 198 | 55% helix, 8% strand | P08263 |
| B | Glutathione S-transferase A1 (EC 2.5.1.18) | protein | 208 | 57% helix, 9% strand | P08263 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.82 | 0.83 | 92 | empty |
| 2 | 99 | 0.36 | 0.74 | 18 | empty |
| 3 | 80 | 0.34 | 0.75 | 24 | empty |
| 4 | 62 | 0.29 | 0.74 | 14 | empty |
| 5 | 66 | 0.28 | 0.72 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1503 Ų buried · 10 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 P08263
- Elsewhere: RCSB PDB 1K3O · PDBe 1K3O · UniProt P08263
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