Research workbench
Crystal structure of PAAZOR1 bound to ubiquinone-1
Analyse Crystal structure of PAAZOR1 bound to ubiquinone-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N9Q
- Type
- protein
- Length
- 397 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN-dependent NADH-azoreductase 1
- EC
- 1.7.-.-
- UniProt
- Q9I5F3
- Ligands
- FMN, UQ1, SO4
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN-dependent NADH-azoreductase 1 (EC 1.7.-.-) | protein | 205 | 42% helix, 21% strand | Q9I5F3 |
| B | FMN-dependent NADH-azoreductase 1 (EC 1.7.-.-) | protein | 192 | 41% helix, 20% strand | Q9I5F3 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- UQ1 · Ubiquinone-1 · ligand · chains A, B
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.74 | 0.83 | 34 | UQ1, FMN |
| 2 | 362 | 0.72 | 0.84 | 33 | FMN |
| 3 | 140 | 0.54 | 0.81 | 39 | GOL |
Interfaces
1 interface between chains.
- A–B · 1310 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 Q9I5F3
- Elsewhere: RCSB PDB 4N9Q · PDBe 4N9Q · UniProt Q9I5F3
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