› 5tr2

X-ray diffraction
2.5Å resolution

Crystal structure of the D263G missense variant of human PGM1

Released:
DOI: 10.2210/pdb5tr2/pdb
PDB entry 5tr2 coloured by chain, front view.
PDB entry 5tr2 coloured by chain, side view.
PDB entry 5tr2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Asp263 missense variants perturb the active site of human phosphoglucomutase 1.
Stiers KM, Graham AC, Kain BN, Beamer LJ
FEBS J 284 937-947 (2017)
PMID: 28117557

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-543654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglucomutase-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 585 amino acids
Theoretical weight: 64.21 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 4 x SO4
Ligand CA 2 x CA
Ligand GOL 1 x GOL
1 modified residue:
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P41212
Unit cell:
a: 172.124Å b: 172.124Å c: 99.005Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.22 0.292
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Sequence-structure relationships, expression profiles, and disease-associated mutations in the paralogs of phosphoglucomutase 1.
Muenks et al. (2017)
7 more

1 mention without citation

Asp263 missense variants perturb the active site of human phosphoglucomutase 1.
Stiers et al. (2017)