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Purification, characterization and X-ray structure of yhda-type azoreductase from bacillus velezensis
Analyse Purification, characterization and X-ray structure of yhda-type azoreductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BX9
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Azoreductase
- UniProt
- B3VPZ9
- Ligands
- FMN, PO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Azoreductase | protein | 168 | 44% helix, 20% strand | B3VPZ9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BX9 · Purification, characterization and X-ray structure of YhdA-type azoreductase from… · 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 B3VPZ9
- Elsewhere: RCSB PDB 7BX9 · PDBe 7BX9 · UniProt B3VPZ9
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