Research workbench
1.88 ångström resolution crystal structure of glutathione reductase from streptococcus mutans UA159 in complex with FAD
Analyse 1.88 ångström resolution crystal structure of glutathione reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V36
- Type
- protein
- Length
- 902 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione reductase
- EC
- 3.3.1.1, 1.8.1.7
- UniProt
- Q8DUR5
- Ligands
- FAD, BDF, SO4, CL
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione reductase (EC 3.3.1.1, 1.8.1.7) | protein | 451 | 36% helix, 26% strand | Q8DUR5 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- BDF · beta-D-fructopyranose · ligand · chains A, B
- SO4 · Sulfate ion · ion · 30 copies · chains A, B
- CL · Chloride ion · ion · 8 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.82 | 0.96 | 43 | BDF |
| 2 | 918 | 0.80 | 0.82 | 109 | FAD, CL, SO4 |
| 3 | 932 | 0.79 | 0.81 | 97 | FAD, CL, SO4 |
| 4 | 733 | 0.73 | 0.79 | 60 | BME, CL, SO4 |
| 5 | 717 | 0.72 | 0.78 | 62 | SO4, BME |
Interfaces
1 interface between chains.
- A–B · 3596 Ų buried · 41 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5V36 · 1.88 Angstrom Resolution Crystal Structure of Glutathione Reductase from Streptococcus… · 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 Q8DUR5
- Elsewhere: RCSB PDB 5V36 · PDBe 5V36 · UniProt Q8DUR5
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