› 2fuc

X-ray diffraction
2.1Å resolution

Human alpha-Phosphomannomutase 1 with Mg2+ cofactor bound

Released:
DOI: 10.2210/pdb2fuc/pdb
PDB entry 2fuc coloured by chain, front view.
PDB entry 2fuc coloured by chain, side view.
PDB entry 2fuc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.
Silvaggi NR, Zhang C, Lu Z, Dai J, Dunaway-Mariano D, Allen KN
J Biol Chem 281 14918-26 (2006)
PMID: 16540464

Function and Biology Details

Reaction catalysed: 
Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187788 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphomannomutase 1 Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 29.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92871 (Residues: 1-262; Coverage: 100%)
Gene names: PMM1, PMMH22
Sequence domains: Eukaryotic phosphomannomutase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P43212
Unit cell:
a: 51.69Å b: 51.69Å c: 215.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.206
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides.
Haeuptle et al. (2009)
4 more

41 mentions without citation

Chemical structures and bioactivities of sulfated polysaccharides from marine algae.
Jiao et al. (2011)
40 more