› 4c80

X-ray diffraction
1.5Å resolution

Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), soaked with hydrogen peroxide

Released:
DOI: 10.2210/pdb4c80/pdb
PDB entry 4c80 coloured by chain, front view.
PDB entry 4c80 coloured by chain, side view.
PDB entry 4c80 coloured by chain, top view.
Source organism: Megalodesulfovibrio gigas
Primary publication:
Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for enzyme activation and inhibition by H(2)O(2).
Marangon J, Correia HD, Brondino CD, Moura JJ, Romão MJ, González PJ, Santos-Silva T
OpenAccess logo PLoS One 8 e83234 (2013)
PMID: 24391748

Function and Biology Details

Reaction catalysed: 
An aldehyde + H(2)O + acceptor = a carboxylate + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175125 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

8 bound ligands:
Ligand FES 2 x FES
Ligand IPA 1 x IPA
Ligand BCT 1 x BCT
Ligand NA 2 x NA
Ligand MG 3 x MG
Ligand CL 3 x CL
Ligand PCD 1 x PCD
Ligand PEO 1 x PEO
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6122
Unit cell:
a: 143.057Å b: 143.057Å c: 162.292Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.105 0.103 0.134

Quick links

Citations

1 review citation

The History of Desulfovibrio gigas Aldehyde Oxidoreductase-A Personal View.
Moura JJG. (2023)
1 other article

2 mentions without citation

Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for enzyme activation and inhibition by H(2)O(2).
Marangon et al. (2013)
1 more