› 5epc

X-ray diffraction
1.85Å resolution

Crystal structure of wild-type human phosphoglucomutase 1

Released:
DOI: 10.2210/pdb5epc/pdb
PDB entry 5epc coloured by chain, front view.
PDB entry 5epc coloured by chain, side view.
PDB entry 5epc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency.
Stiers KM, Kain BN, Graham AC, Beamer LJ
J Mol Biol 428 1493-505 (2016)
PMID: 26972339

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 BL21(DE3)
UniProt:
  • Canonical: P36871 (Residues: 1-562; Coverage: 100%)
Gene name: PGM1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand SO4 8 x SO4
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 172.59Å b: 172.59Å c: 99.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Liver glucose metabolism in humans.
Adeva-Andany et al. (2016)
3 other articles

11 mentions without citation

Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.
Stiers et al. (2017)
10 more