› 6uiq

X-ray diffraction
2.3Å resolution

Crystal structure of wild-type human phosphoglucomutase 1 in complex with Glucose-6-Phosphate

Released:
DOI: 10.2210/pdb6uiq/pdb
PDB entry 6uiq coloured by chain, front view.
PDB entry 6uiq coloured by chain, side view.
PDB entry 6uiq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Hotspot for Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics.
Stiers KM, Beamer LJ
Structure 26 1337-1345.e3 (2018)
PMID: 30122451

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 585 amino acids
Theoretical weight: 64.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36871 (Residues: 1-562; Coverage: 100%)
Gene name: PGM1
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand G6P 2 x G6P
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 171.874Å b: 171.874Å c: 99.447Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.168 0.223
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Structural and dynamical description of the enzymatic reaction of a phosphohexomutase.
Stiers et al. (2019)
7 more

2 mentions without citation

Genetic validation of Aspergillus fumigatus phosphoglucomutase as a viable therapeutic target in invasive aspergillosis.
Yan et al. (2022)
1 more