1oqc

X-ray diffraction
1.8Å resolution

The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase

Released:
Source organism: Rattus norvegicus
Primary publication:
The refined crystal structure of augmenter of liver regeneration
Int. Union Cryst. (Meeting) 1 293-293 (1999)

Function and Biology Details

Reaction catalysed:
2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + H(2)O(2)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-linked sulfhydryl oxidase ALR Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 125 amino acids
Theoretical weight: 15.1 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q63042 (Residues: 74-198; Coverage: 63%)
Gene names: Alr, Gfer
Sequence domains: Erv1 / Alr family
Structure domains: ERV/ALR sulfhydryl oxidase domain

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C, APS BEAMLINE 17-ID
Spacegroup: P21212
Unit cell:
a: 106.987Å b: 123.13Å c: 37.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.24
Expression system: Escherichia coli BL21