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Crystal structure of a genetically modified delta class GST (ADGSTD4- 4) from anopheles dirus, F123A, in complex with S-hexyl glutathione
Analyse Crystal structure of a genetically modified delta class GST (ADGSTD4- 4) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F6D
- Type
- protein
- Length
- 421 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase GST1-4
- EC
- 2.5.1.18
- UniProt
- Q9GN60
- Ligands
- GTX
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione transferase GST1-4 (EC 2.5.1.18) | protein | 218 | 62% helix, 6% strand | Q9GN60 |
| B | Glutathione transferase GST1-4 (EC 2.5.1.18) | protein | 203 | 64% helix, 7% strand | Q9GN60 |
Ligands and binding sites
- GTX · S-hexylglutathione · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 688 | 0.74 | 0.80 | 45 | GTX |
| 2 | 482 | 0.67 | 0.78 | 42 | GTX |
| 3 | 89 | 0.37 | 0.76 | 20 | empty |
| 4 | 61 | 0.36 | 0.78 | 18 | empty |
| 5 | 92 | 0.34 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1534 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3F6D · Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles… · 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 Q9GN60
- Elsewhere: RCSB PDB 3F6D · PDBe 3F6D · UniProt Q9GN60
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