Research workbench
Crystal structure of a glutathione S-transferase protein from escherichia COLI och 157:H7 str. sakai (ECS3186, target efi-507414) with bound glutathione
Analyse Crystal structure of a glutathione S-transferase protein from escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HFK
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disulfide-bond oxidoreductase yfcg
- EC
- 1.8.4.-, 1.11.1.-
- UniProt
- P77526
- Ligands
- GSH
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disulfide-bond oxidoreductase yfcg (EC 1.8.4.-, 1.11.1.-) | protein | 207 | 60% helix, 10% strand | P77526 |
| B | Disulfide-bond oxidoreductase yfcg (EC 1.8.4.-, 1.11.1.-) | protein | 205 | 60% helix, 10% strand | P77526 |
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
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 445 | 0.71 | 0.81 | 36 | GSH |
| 2 | 452 | 0.70 | 0.81 | 37 | GSH |
| 3 | 119 | 0.41 | 0.75 | 21 | empty |
| 4 | 110 | 0.39 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2016 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 5HFK · CRYSTAL STRUCTURE OF A GLUTATHIONE S-TRANSFERASE PROTEIN FROM ESCHERICHIA COLI OCh 157:H7… · the same entry in another collection · chain A against A, TM-score 1.00
- P77526 · AlphaFold monomer V2.0 prediction for disulfide-bond oxidoreductase yfcg (P77526) · a predicted model of the same protein · 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 P77526
- Elsewhere: RCSB PDB 5HFK · PDBe 5HFK · UniProt P77526
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