Research workbench
Glutathione S-transferase 1-6 from anopheles dirus species B
Analyse Glutathione S-transferase 1-6 from anopheles dirus species B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V2A
- Type
- protein
- Length
- 833 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase GST1-6
- EC
- 2.5.1.18
- UniProt
- Q9BHB0
- Ligands
- GTS
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Glutathione transferase GST1-6 (EC 2.5.1.18) | protein | 208 | 60% helix, 8% strand | Q9BHB0 |
| B | Glutathione transferase GST1-6 (EC 2.5.1.18) | protein | 209 | 60% helix, 8% strand | Q9BHB0 |
Ligands and binding sites
- GTS · Glutathione sulfonic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.77 | 0.79 | 99 | GTS |
| 2 | 1065 | 0.77 | 0.79 | 83 | GTS |
| 3 | 87 | 0.43 | 0.79 | 21 | empty |
| 4 | 88 | 0.42 | 0.79 | 16 | empty |
| 5 | 73 | 0.32 | 0.74 | 13 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1365 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 1362 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1V2A · Glutathione S-transferase 1-6 from Anopheles dirus species B · the same entry in another collection · 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 Q9BHB0
- Elsewhere: RCSB PDB 1V2A · PDBe 1V2A · UniProt Q9BHB0
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