Research workbench
Structure of glutathione S-transferase III in apo form
Analyse Structure of glutathione S-transferase III in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AW9
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase III
- EC
- 2.5.1.18
- UniProt
- Q9ZP62
- Ligands
- CD
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase III (EC 2.5.1.18) | protein | 216 | 55% helix, 8% strand | Q9ZP62 |
Ligands and binding sites
- CD · Cadmium ion · metal · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.41 | 0.74 | 21 | empty |
Compared structures
- 1AW9 · Structure of glutathione S-transferase III in apo form · 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 Q9ZP62
- Elsewhere: RCSB PDB 1AW9 · PDBe 1AW9 · UniProt Q9ZP62
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