Research workbench
Crystal structure of equus ferus caballus glutathione transferase A3-3 in complex with glutathione
Analyse Crystal structure of equus ferus caballus glutathione transferase A3-3 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZJ9
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- M9ZT87
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 220 | 58% helix, 8% strand | M9ZT87 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.69 | 0.80 | 40 | GSH |
| 2 | 120 | 0.68 | 0.90 | 21 | EDO |
| 3 | 54 | 0.28 | 0.74 | 12 | empty |
Compared structures
- 6ZJ9 · Crystal structure of Equus ferus caballus glutathione transferase A3-3 in complex with… · 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 M9ZT87
- Elsewhere: RCSB PDB 6ZJ9 · PDBe 6ZJ9 · UniProt M9ZT87
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