› 3lli

X-ray diffraction
2.05Å resolution

Sulfhydryl Oxidase Fragment of Human QSOX1

Released:
DOI: 10.2210/pdb3lli/pdb
PDB entry 3lli coloured by chain, front view.
PDB entry 3lli coloured by chain, side view.
PDB entry 3lli coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains.
Alon A, Heckler EJ, Thorpe C, Fass D
FEBS Lett 584 1521-5 (2010)
PMID: 20211621

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfhydryl oxidase 1 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00391 (Residues: 286-546; Coverage: 36%)
Gene names: QSCN6, QSOX1, UNQ2520/PRO6013
Sequence domains:
Structure domains:

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: RIGAKU RUH3R
Spacegroup: P6422
Unit cell:
a: 85.606Å b: 85.606Å c: 125.706Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.275 0.275 0.324
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structure, mechanism, and evolution of Ero1 family enzymes.
Araki et al. (2012)
8 more

1 mention without citation

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
Fass et al. (2018)