Research workbench
Crystallographic structure of the tau class glutathione S-transferase migstu from mango mangifera indica L.
Analyse Crystallographic structure of the tau class glutathione S-transferase migstu… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G5E
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tau class glutathione S-transferase
- EC
- 2.5.1.18
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tau class glutathione S-transferase (EC 2.5.1.18) | protein | 220 | 55% helix, 9% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.54 | 0.74 | 39 | ACT |
| 2 | 110 | 0.43 | 0.77 | 27 | empty |
Compared structures
- 5G5E · Crystallographic structure of the Tau class glutathione S-transferase MiGSTU from mango… · 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
- Elsewhere: RCSB PDB 5G5E · PDBe 5G5E
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