Research workbench
Crystal structure of a glutathione S-transferase class GTT2 of vibrio parahaemolyticus (VPGSTT2)
Analyse Crystal structure of a glutathione S-transferase class GTT2 of vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MIQ
- Type
- protein
- Length
- 407 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- A0A2R9VI90
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 207 | 56% helix, 8% strand | A0A2R9VI90 |
| B | Glutathione S-transferase (EC 2.5.1.18) | protein | 200 | 57% helix, 8% strand | A0A2R9VI90 |
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 | 989 | 0.81 | 0.82 | 97 | PEG |
| 2 | 177 | 0.50 | 0.77 | 31 | PEG |
| 3 | 80 | 0.39 | 0.78 | 20 | empty |
| 4 | 66 | 0.29 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1732 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 7MIQ · Crystal structure of a Glutathione S-transferase class Gtt2 of Vibrio parahaemolyticus… · 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 A0A2R9VI90
- Elsewhere: RCSB PDB 7MIQ · PDBe 7MIQ · UniProt A0A2R9VI90
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