MolNFT v1 · #135526 · protein
2.3 ångström resolution crystal structure of glutathione reductase from vibrio parahaemolyticus in complex with FAD.
5U1O: “2.3 ångström resolution crystal structure of glutathione reductase from vibrio parahaemolyticus in complex…”. X-ray diffraction, 3 ligands (FAD, SO4, CL), 8 pockets (best druggability 0.86). MolNFT v1 #135526 on GenesisL1: 3D…
- PDB
- 5U1O
- Type
- protein
- Length
- 1,802 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione reductase
- UniProt
- Q87TK1
- Ligands
- FAD, SO4, CL
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Glutathione reductase | protein | 450 | 35% helix, 28% strand | Q87TK1 |
| B, C | Glutathione reductase | protein | 451 | 35% helix, 27% strand | Q87TK1 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.86 | 0.87 | 142 | empty |
| 2 | 1013 | 0.85 | 0.86 | 150 | empty |
| 3 | 812 | 0.79 | 0.82 | 92 | FAD |
| 4 | 791 | 0.79 | 0.82 | 91 | FAD, CL |
| 5 | 829 | 0.78 | 0.81 | 97 | FAD |
Interfaces
6 interfaces between chains.
- A–B · 3612 Ų buried · 36 hydrogen bonds · protein-protein
- C–D · 3580 Ų buried · 33 hydrogen bonds · protein-protein
- B–C · 423 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 410 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 20 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5U1O · 2.3 Angstrom Resolution Crystal Structure of Glutathione Reductase from Vibrio… · 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 Q87TK1
- Elsewhere: RCSB PDB 5U1O · PDBe 5U1O · UniProt Q87TK1
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