3o55

X-ray diffraction
1.9Å resolution

Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)

Released:

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-linked sulfhydryl oxidase ALR Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 14.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55789 (Residues: 81-205; Coverage: 61%)
Gene names: ALR, GFER, HERV1, HPO
Sequence domains: Erv1 / Alr family
Structure domains: ERV/ALR sulfhydryl oxidase domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: C2221
Unit cell:
a: 50.849Å b: 76.566Å c: 62.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.182 0.267
Expression system: Escherichia coli