› 6sno

X-ray diffraction
2.7Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153233 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglucomutase-1 Chain: A
Molecule details ›
Chain: A
Length: 583 amino acids
Theoretical weight: 64.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36871 (Residues: 2-562; Coverage: 100%)
Gene name: PGM1
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand G1P 1 x G1P
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 72.954Å b: 53.351Å c: 76.321Å
α: 90° β: 98.44° γ: 90°
R-values:
R R work R free
0.2 0.197 0.248
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Glucose-1,6-Bisphosphate, a Key Metabolic Regulator, Is Synthesized by a Distinct Family of α-Phosphohexomutases Widely Distributed in Prokaryotes.
Neumann et al. (2022)
3 more

2 mentions without citation

Structural basis for substrate and product recognition in human phosphoglucomutase-1 (PGM1) isoform 2, a member of the α-D-phosphohexomutase superfamily.
Backe et al. (2020)
1 more