› 6t85

X-ray diffraction
1.1Å resolution

Function and Biology Details

Reaction catalysed: 
Dihydrourocanate + acceptor = urocanate + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Urocanate reductase Chain: A
Molecule details ›
Chain: A
Length: 460 amino acids
Theoretical weight: 49.98 KDa
Source organism: Shewanella oneidensis MR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8CVD0 (Residues: 130-582; Coverage: 81%)
Gene names: SO_4620, urdA
Sequence domains: FAD binding domain

Ligands and Environments

3 bound ligands:
Ligand ADP 1 x ADP
Ligand CL 5 x CL
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P21
Unit cell:
a: 41.839Å b: 95.762Å c: 63.2Å
α: 90° β: 91.04° γ: 90°
R-values:
R R work R free
0.109 0.108 0.13
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Dali server: structural unification of protein families.
Holm L. (2022)
2 more

1 mention without citation

Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production.
Venskutonytė et al. (2021)