Research workbench
Structures of an Insect Epsilon-class Glutathione S-transferase from the Malaria Vector Anopheles Gambiae: Evidence for High DDT-detoxifying Activity
Analyse Structures of an Insect Epsilon-class Glutathione S-transferase from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IL3
- Type
- protein
- Length
- 438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Anopheles gambiae
- Molecule
- Epsilon-class Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- Q7PVS6
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epsilon-class Glutathione S-transferase (EC 2.5.1.18) | protein | 220 | 55% helix, 8% strand | Q7PVS6 |
| B | Epsilon-class Glutathione S-transferase (EC 2.5.1.18) | protein | 218 | 59% helix, 9% strand | Q7PVS6 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.81 | 0.88 | 53 | empty |
| 2 | 396 | 0.79 | 0.88 | 49 | empty |
| 3 | 191 | 0.54 | 0.79 | 30 | empty |
| 4 | 130 | 0.53 | 0.81 | 20 | empty |
| 5 | 80 | 0.41 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1675 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2IL3 · Structures of an insect epsilon-class glutathione S-transferase from the malaria vector… · 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 Q7PVS6
- Elsewhere: RCSB PDB 2IL3 · PDBe 2IL3 · UniProt Q7PVS6
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