› 5hsh

X-ray diffraction
2.65Å resolution

Crystal structure of the G291R mutant of human phosphoglucomutase 1

Released:
DOI: 10.2210/pdb5hsh/pdb
PDB entry 5hsh coloured by chain, front view.
PDB entry 5hsh coloured by chain, side view.
PDB entry 5hsh 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: 562 amino acids
Theoretical weight: 61.62 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

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 170.78Å b: 170.78Å c: 99.287Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

2 mentions without citation

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