› 5vin

X-ray diffraction
2.6Å resolution

Crystal Structure of the R515Q missense variant of human PGM1

Released:
DOI: 10.2210/pdb5vin/pdb
PDB entry 5vin coloured by chain, front view.
PDB entry 5vin coloured by chain, side view.
PDB entry 5vin 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: 64.16 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 SO4 13 x SO4
Ligand GOL 6 x GOL
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 173.96Å b: 173.96Å c: 99.483Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.239 0.295
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

1 mention without citation

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