› 2q4r

X-ray diffraction
2.09Å resolution

Ensemble refinement of the protein crystal structure of human phosphomannomutase 2 (PMM2)

Released:
DOI: 10.2210/pdb2q4r/pdb
PDB entry 2q4r coloured by chain, ensemble of 16 models, front view.
PDB entry 2q4r coloured by chain, ensemble of 16 models, side view.
PDB entry 2q4r coloured by chain, ensemble of 16 models, top view.
Source organism: Homo sapiens
Primary publication:
Ensemble refinement of protein crystal structures: validation and application.
Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN
Structure 15 1040-52 (2007)
PMID: 17850744

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphomannomutase 2 Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 28.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15305 (Residues: 2-246; Coverage: 100%)
Gene name: PMM2
Sequence domains: Eukaryotic phosphomannomutase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EDO 1 x EDO
Ligand GLY 3 x GLY
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 70.622Å b: 70.622Å c: 100.15Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.207 0.298
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Enzymes in jasmonate biosynthesis - structure, function, regulation.
Schaller et al. (2009)
18 more

1 mention without citation

Biochemical phenotype of a common disease-causing mutation and a possible therapeutic approach for the phosphomannomutase 2-associated disorder of glycosylation.
Andreotti et al. (2013)