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Anopheles funestus glutathione-S-transferase epsilon 2 (GSTE2) protein structure from different alelles: a single amino acid change confers high level of ddt resistance and cross resistance to permethrin in a major malaria vector in africa
Analyse Anopheles funestus glutathione-S-transferase epsilon 2 (GSTE2) protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZMK
- Type
- protein
- Length
- 842 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase E2
- UniProt
- G0XSZ1
- Ligands
- GSH
- Pockets
- 11 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase E2 | protein | 200 | 60% helix, 10% strand | G0XSZ1 |
| B | Glutathione S-transferase E2 | protein | 222 | 59% helix, 9% strand | G0XSZ1 |
| C | Glutathione S-transferase E2 | protein | 199 | 59% helix, 9% strand | G0XSZ1 |
| D | Glutathione S-transferase E2 | protein | 221 | 59% helix, 9% strand | G0XSZ1 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 793 | 0.86 | 0.89 | 84 | GSH |
| 2 | 886 | 0.79 | 0.81 | 58 | GSH |
| 3 | 331 | 0.70 | 0.83 | 45 | empty |
| 4 | 456 | 0.67 | 0.79 | 37 | empty |
| 5 | 111 | 0.53 | 0.83 | 22 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1664 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 1347 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 303 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 235 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 133 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3ZMK · Anopheles funestus glutathione-s-transferase epsilon 2 (GSTe2) protein structure from… · 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 G0XSZ1
- Elsewhere: RCSB PDB 3ZMK · PDBe 3ZMK · UniProt G0XSZ1
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