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Crystal structure analysis of yghu from E. COLI
Analyse Crystal structure analysis of yghu from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C8E
- Type
- protein
- Length
- 567 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yghu, glutathione S-transferase homologue
- UniProt
- Q46845
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Yghu, glutathione S-transferase homologue | protein | 284 | 49% helix, 9% strand | Q46845 |
| B | Yghu, glutathione S-transferase homologue | protein | 283 | 50% helix, 9% strand | Q46845 |
Ligands and binding sites
- GSH · Glutathione · ligand · 4 copies · chains A, B
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 | 761 | 0.83 | 0.86 | 66 | GSH |
| 2 | 796 | 0.82 | 0.85 | 79 | GSH |
| 3 | 57 | 0.25 | 0.72 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 3308 Ų buried · 49 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 Q46845
- Elsewhere: RCSB PDB 3C8E · PDBe 3C8E · UniProt Q46845
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