PDBsum entry 1sij

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Oxidoreductase PDB id
Jmol PyMol
Protein chain
907 a.a. *
FES ×2
_CL ×3
_MG ×2
Waters ×414
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal structure of the aldehyde dehydrogenase (a.K.A. Aor or mop) of desulfovibrio gigas covalently bound to [aso3]-
Structure: Aldehyde oxidoreductase. Chain: a. Synonym: molybdenum iron sulfur protein. Aldehyde oxidase. Aldehyde dehydrogenase. Other_details: biologically relevant dimer cannot be unequivocally identified in the crystal
Source: Desulfovibrio gigas. Organism_taxid: 879
2.30Å     R-factor:   0.207     R-free:   0.223
Authors: D.R.Boer,A.Thapper,C.D.Brondino,M.J.Romao,J.J.G.Moura
Key ref: D.R.Boer et al. (2004). X-ray crystal structure and EPR spectra of "arsenite-inhibited" Desulfovibriogigas aldehyde dehydrogenase: a member of the xanthine oxidase family. J Am Chem Soc, 126, 8614-8615. PubMed id: 15250689 DOI: 10.1021/ja0490222
01-Mar-04     Release date:   27-Jul-04    
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Protein chain
Pfam   ArchSchema ?
Q46509  (MOP_DESGI) -  Aldehyde oxidoreductase
907 a.a.
907 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Aldehyde dehydrogenase (FAD-independent).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An aldehyde + H2O + acceptor = a carboxylate + reduced acceptor
+ H(2)O
+ acceptor
= carboxylate
+ reduced acceptor
      Cofactor: Iron-sulfur; Molybdopterin cytosine dinucleotide
Bound ligand (Het Group name = PCD) matches with 58.00% similarity
Molybdopterin cytosine dinucleotide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     electron carrier activity     6 terms  


DOI no: 10.1021/ja0490222 J Am Chem Soc 126:8614-8615 (2004)
PubMed id: 15250689  
X-ray crystal structure and EPR spectra of "arsenite-inhibited" Desulfovibriogigas aldehyde dehydrogenase: a member of the xanthine oxidase family.
D.R.Boer, A.Thapper, C.D.Brondino, M.J.Romão, J.J.Moura.
X-ray crystallography has been used to determine the structure of arsenite-inhibited aldehyde dehydrogenase from Desulfovibrio gigas, a member of the xanthine oxidase family of mononuclear molybdenum enzymes. The structure shows an AsO3 moiety bound to the molybdenum atom of the active site through one of the oxygen atoms. A reduced sample of arsenite-inhibited aldehyde dehydrogenase has a Mo(V) signal that shows anisotropic hyperfine and quadrupole coupling to one arsenic atom. This signal has a strong resemblance with a previously reported signal for arsenite-inhibited xanthine oxidase.

Literature references that cite this PDB file's key reference

  PubMed id Reference
17139522 A.Thapper, D.R.Boer, C.D.Brondino, J.J.Moura, and M.J.Romão (2007).
Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase.
  J Biol Inorg Chem, 12, 353-366.
PDB code: 3l4p
16480912 C.D.Brondino, M.J.Romão, I.Moura, and J.J.Moura (2006).
Molybdenum and tungsten enzymes: the xanthine oxidase family.
  Curr Opin Chem Biol, 10, 109-114.  
  16508115 D.R.Boer, A.Müller, S.Fetzner, D.J.Lowe, and M.J.Romão (2005).
On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 137-140.  
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