› 2ati

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139193 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, liver form Chains: A, B
Molecule details ›
Chains: A, B
Length: 846 amino acids
Theoretical weight: 97.15 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P06737 (Residues: 2-847; Coverage: 100%)
Gene name: PYGL
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
2 bound ligands:
Ligand GLC 2 x GLC
Ligand IHU 2 x IHU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P31
Unit cell:
a: 124.5Å b: 124.5Å c: 123.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.232 0.256
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
6 more

1 mention without citation

Azido derivatives of low-valent group 14 elements: synthesis, characterization, and electronic structure of [(n-Pr)2ATI]GeN3 and [(n-Pr)2ATI]SnN3 featuring heterobicyclic 10-pi-electron ring systems.
Ayers et al. (2000)