› 1ygp

X-ray diffraction
2.8Å resolution

PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.

Released:
DOI: 10.2210/pdb1ygp/pdb
PDB entry 1ygp coloured by chain, front view.
PDB entry 1ygp coloured by chain, side view.
PDB entry 1ygp coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A protein phosphorylation switch at the conserved allosteric site in GP.
Lin K, Rath VL, Dai SC, Fletterick RJ, Hwang PK
Science 273 1539-42 (1996)
PMID: 8703213

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-139196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 879 amino acids
Theoretical weight: 101.28 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P06738 (Residues: 24-902; Coverage: 98%)
Gene names: GPH1, P9584.1, YPR160W
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 103.91Å b: 143.93Å c: 169.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.239
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

3 mentions without citation

Coherent conformational degrees of freedom as a structural basis for allosteric communication.
Mitternacht et al. (2011)
2 more