› 1aor

X-ray diffraction
2.3Å resolution

STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE

Released:
DOI: 10.2210/pdb1aor/pdb
PDB entry 1aor coloured by chain, front view.
PDB entry 1aor coloured by chain, side view.
PDB entry 1aor coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.
Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC
Science 267 1463-9 (1995)
PMID: 7878465

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175968 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tungsten-containing aldehyde ferredoxin oxidoreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 605 amino acids
Theoretical weight: 66.72 KDa
Source organism: Pyrococcus furiosus
Expression system: Not provided
UniProt:
  • Canonical: Q51739 (Residues: 1-605; Coverage: 100%)
Gene names: PF0346, aor
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FE 1 x FE
Ligand NA 2 x NA
Ligand SF4 2 x SF4
Ligand PTE 2 x PTE
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 80.939Å b: 108.332Å c: 159.792Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.155 not available
Expression system: Not provided

Quick links

Citations

48 review citations

Cell biology and molecular basis of denitrification.
Zumft WG. (1997)
47 more

15 mentions without citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
14 more