› 5vg7

X-ray diffraction
1.95Å resolution

Crystal Structure of the R503Q missense variant of human PGM1

Released:
DOI: 10.2210/pdb5vg7/pdb
PDB entry 5vg7 coloured by chain, front view.
PDB entry 5vg7 coloured by chain, side view.
PDB entry 5vg7 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:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphoglucomutase-1 Chain: A
Molecule details ›
Chain: A
Length: 564 amino acids
Theoretical weight: 61.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36871 (Residues: 1-562; Coverage: 100%)
Gene name: PGM1
Sequence domains:
Structure domains:
Phosphoglucomutase-1 Chain: B
Molecule details ›
Chain: B
Length: 564 amino acids
Theoretical weight: 61.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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 18 x SO4
Ligand GOL 5 x GOL
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 172.131Å b: 172.131Å c: 99.805Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.213
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

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

2 mentions without citation

A Hotspot for Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics.
Stiers et al. (2018)
1 more