› 1y1e

X-ray diffraction
1.73Å resolution

Function and Biology Details

Reaction catalysed: 
A [sulfatase]-L-cysteine + O(2) + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H(2)O
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formylglycine-generating enzyme Chain: X
Molecule details ›
Chain: X
Length: 311 amino acids
Theoretical weight: 34.91 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q8NBK3 (Residues: 73-374; Coverage: 89%)
Gene names: PSEC0152, SUMF1, UNQ3037/PRO9852
Sequence domains: Sulfatase-modifying factor enzyme 1
Structure domains: paralog of FGE (formylglycine-generating enzyme)

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21212
Unit cell:
a: 61.956Å b: 110.014Å c: 43.474Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.242
Expression system: Homo sapiens

Quick links

Citations

28 review citations

Radical S-adenosylmethionine enzymes.
Broderick et al. (2014)
27 more

10 mentions without citation

Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.
Appel et al. (2015)
9 more