› 1nxc

X-ray diffraction
1.51Å resolution

Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)

Released:
DOI: 10.2210/pdb1nxc/pdb
PDB entry 1nxc coloured by chain, front view.
PDB entry 1nxc coloured by chain, side view.
PDB entry 1nxc coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases.
Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW
J. Biol. Chem. 279 29774-86 (2004)
PMID: 15102839

Function and Biology Details

Reaction catalysed: 
(1a) Man(9)GlcNAc(2)-[protein] + H(2)O = Man(8)GlcNAc(2)-[protein] (isomer 8A(1,2,3)B(1,2)) + beta-D-mannopyranose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 54.54 KDa
Source organism: Mus musculus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P45700 (Residues: 178-655; Coverage: 73%)
Gene names: Man1a, Man1a1
Sequence domains: Glycosyl hydrolase family 47
Structure domains: Glycosyltransferase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P212121
Unit cell:
a: 55.288Å b: 72.164Å c: 129.571Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.19
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

In and out of the ER: protein folding, quality control, degradation, and related human diseases.
Hebert et al. (2007)
3 more

4 mentions without citation

NetCSSP: web application for predicting chameleon sequences and amyloid fibril formation.
Kim et al. (2009)
3 more