Research workbench
Crystal structure of escherichia COLI quinone oxidoreductase complexed with NADPH
Analyse Crystal structure of escherichia COLI quinone oxidoreductase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QOR
- Type
- protein
- Length
- 652 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Quinone oxidoreductase
- UniProt
- P28304
- Ligands
- NDP, SO4
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Quinone oxidoreductase | protein | 326 | 35% helix, 25% strand | P28304 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 544 | 0.80 | 0.86 | 62 | SO4, NDP |
| 2 | 608 | 0.79 | 0.84 | 59 | SO4, NDP |
| 3 | 129 | 0.38 | 0.73 | 17 | empty |
| 4 | 58 | 0.36 | 0.79 | 18 | empty |
| 5 | 60 | 0.36 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1254 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 1QOR · Crystal structure of escherichia COLI quinone oxidoreductase complexed with NADPH · the same entry in another collection · chain A against A, TM-score 1.00
- P28304 · AlphaFold monomer V2.0 prediction for quinone oxidoreductase 1 (P28304) · 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 P28304
- Elsewhere: RCSB PDB 1QOR · PDBe 1QOR · UniProt P28304
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