› 6cfu

X-ray diffraction
2.24Å resolution

Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K

Released:
DOI: 10.2210/pdb6cfu/pdb
PDB entry 6cfu coloured by chain, front view.
PDB entry 6cfu coloured by chain, side view.
PDB entry 6cfu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions.
Ji T, Zhang C, Zheng L, Dunaway-Mariano D, Allen KN
Biochemistry 57 3480-3492 (2018)
PMID: 29695157

Function and Biology Details

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

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: 29.73 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
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P43212
Unit cell:
a: 50.65Å b: 50.65Å c: 213.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.217 0.274
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Impaired glucose-1,6-biphosphate production due to bi-allelic PGM2L1 mutations is associated with a neurodevelopmental disorder.
Morava et al. (2021)
2 more

1 mention without citation

Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions.
Ji et al. (2018)