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Crystal structure of HGSTA3-3 in complex with glutathione
Analyse Crystal structure of HGSTA3-3 in complex with glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TDI
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase A3-3
- EC
- 2.5.1.18
- UniProt
- Q16772
- Ligands
- GSH
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase A3-3 (EC 2.5.1.18) | protein | 218 | 60% helix, 7% strand | Q16772 |
Ligands and binding sites
- GSH · Glutathione · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1081 | 0.83 | 0.84 | 110 | GSH |
| 2 | 79 | 0.47 | 0.82 | 27 | empty |
| 3 | 123 | 0.39 | 0.74 | 20 | empty |
| 4 | 123 | 0.38 | 0.74 | 18 | empty |
| 5 | 52 | 0.28 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1559 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 Q16772
- Elsewhere: RCSB PDB 1TDI · PDBe 1TDI · UniProt Q16772
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