MolNFT v1 · #118394 · protein
Structure of the glutathione transferase delta 2 from drosophila melanogaster
5F0G · Glutathione S-transferase D2: “Structure of the glutathione transferase delta 2 from drosophila melanogaster”. X-ray diffraction, 2 ligands (NA, K), 4 pockets (best druggability 0.76). MolNFT v1 #118394 on GenesisL1: 3D structure…
- PDB
- 5F0G
- Type
- protein
- Length
- 409 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase D2
- EC
- 2.5.1.18
- UniProt
- Q9VG98
- Ligands
- NA, K
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase D2 (EC 2.5.1.18) | protein | 207 | 61% helix, 10% strand | Q9VG98 |
| B | Glutathione S-transferase D2 (EC 2.5.1.18) | protein | 202 | 60% helix, 10% strand | Q9VG98 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 927 | 0.76 | 0.79 | 94 | NA |
| 2 | 108 | 0.37 | 0.74 | 18 | empty |
| 3 | 78 | 0.33 | 0.75 | 22 | empty |
| 4 | 76 | 0.30 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1477 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5F0G · Structure of the glutathione transferase delta 2 from Drosophila melanogaster · the same entry in another collection · chain A against A, TM-score 1.00
- Q9VG98 · AlphaFold monomer V2.0 prediction for glutathione S-transferase D2 (Q9VG98) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9VG98
- Elsewhere: RCSB PDB 5F0G · PDBe 5F0G · UniProt Q9VG98
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