PDBe 1fmi

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF HUMAN CLASS I ALPHA1,2-MANNOSIDASE

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase Chain: A
Molecule details ›
Chain: A
Length: 458 amino acids
Theoretical weight: 52.58 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q9UKM7 (Residues: 242-697; Coverage: 65%)
Gene names: MAN1B1, UNQ747/PRO1477
Sequence domains: Glycosyl hydrolase family 47
Structure domains: Glycosyltransferase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P3121
Unit cell:
a: 95.829Å b: 95.829Å c: 136.853Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.222 0.25
Expression system: Saccharomyces cerevisiae