Research workbench
Crystal structure of mouse NAD[P]H-quinone oxidoreductase
Analyse Crystal structure of mouse NAD[P]H-quinone oxidoreductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DXQ
- Type
- protein
- Length
- 1,092 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Quinone reductase
- EC
- 1.6.99.2
- UniProt
- Q64669
- Ligands
- FAD
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Quinone reductase (EC 1.6.99.2) | protein | 273 | 37% helix, 16% strand | Q64669 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 857 | 0.82 | 0.84 | 92 | empty |
| 2 | 593 | 0.78 | 0.84 | 50 | FAD |
| 3 | 587 | 0.78 | 0.84 | 47 | FAD |
| 4 | 94 | 0.77 | 0.97 | 20 | empty |
| 5 | 100 | 0.77 | 0.97 | 19 | empty |
Interfaces
5 interfaces between chains.
- B–D · 2845 Ų buried · 34 hydrogen bonds · protein-protein
- A–C · 2825 Ų buried · 33 hydrogen bonds · protein-protein
- A–D · 438 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 325 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 80 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1DXQ · Crystal structure of mouse NAD[P]H-quinone oxidoreductase · the same entry in another collection · chain A against A, TM-score 1.00
- Q64669 · AlphaFold monomer V2.0 prediction for NAD(P)H dehydrogenase [quinone] 1 (Q64669) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q64669
- Elsewhere: RCSB PDB 1DXQ · PDBe 1DXQ · UniProt Q64669
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