› 4us8

X-ray diffraction
1.49Å resolution

Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), soaked with benzaldehyde

Released:
DOI: 10.2210/pdb4us8/pdb
PDB entry 4us8 coloured by chain, front view.
PDB entry 4us8 coloured by chain, side view.
PDB entry 4us8 coloured by chain, top view.
Source organism: Megalodesulfovibrio gigas
Primary publication:
Aromatic aldehydes at the active site of aldehyde oxidoreductase from Desulfovibrio gigas: reactivity and molecular details of the enzyme-substrate and enzyme-product interaction.
Correia HD, Marangon J, Brondino CD, Moura JJ, Romão MJ, González PJ, Santos-Silva T
J Biol Inorg Chem 20 219-29 (2015)
PMID: 25261288

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 PGE 1 x PGE
Ligand IPA 1 x IPA
Ligand BCT 1 x BCT
Ligand MG 4 x MG
Ligand CL 2 x CL
Ligand PCD 1 x PCD
Ligand HBX 4 x HBX
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: 143.229Å b: 143.229Å c: 162.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.093 0.091 0.122

Quick links

Citations

1 review citation

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

1 mention without citation

Archaeal Mo-Containing Glyceraldehyde Oxidoreductase Isozymes Exhibit Diverse Substrate Specificities through Unique Subunit Assemblies.
Wakagi et al. (2016)