1z70

X-ray diffraction
1.15Å resolution

1.15A resolution structure of the formylglycine generating enzyme FGE

Released:
Source organism: Homo sapiens
Primary publication:
De novo calcium/sulfur SAD phasing of the human formylglycine-generating enzyme using in-house data.
Acta Crystallogr D Biol Crystallogr 61 1057-66 (2005)
PMID: 16041070

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-185466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Formylglycine-generating enzyme Chain: X
Molecule details ›
Chain: X
Length: 311 amino acids
Theoretical weight: 35 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

Carbohydrate polymer : NEW Components: NAG
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21212
Unit cell:
a: 62.295Å b: 109.765Å c: 43.511Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.138 0.17
Expression system: Homo sapiens