› 6snp

X-ray diffraction
2.75Å 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: 64.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36871 (Residues: 2-562; Coverage: 100%)
  • Best match: P36871-2 (Residues: 2-580)
Gene name: PGM1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 72.339Å b: 53.382Å c: 76.066Å
α: 90° β: 100.15° γ: 90°
R-values:
R R work R free
0.212 0.209 0.27
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

PGM1 and ENO1 Promote the Malignant Progression of Bladder Cancer via Comprehensive Analysis of the m6A Signature and Tumor Immune Infiltration.
Zhao et al. (2022)
4 more

1 mention 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)