Research workbench
Crystal structure of glutathione S-transferase B4XH91 (target efi- 501787) from actinobacillus pleuropneumoniae
Analyse Crystal structure of glutathione S-transferase B4XH91 (target efi- 501787) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HZ4
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione-S-transferase
- UniProt
- B4XH91
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione-S-transferase | protein | 215 | 54% helix, 9% strand | B4XH91 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
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 | 175 | 0.55 | 0.80 | 27 | empty |
| 2 | 50 | 0.26 | 0.74 | 11 | empty |
Compared structures
- 4HZ4 · Crystal structure of glutathione s-transferase b4xh91 (target efi-501787) from… · 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 B4XH91
- Elsewhere: RCSB PDB 4HZ4 · PDBe 4HZ4 · UniProt B4XH91
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.