5lr8

X-ray diffraction
2.7Å resolution

Structure of plastidial phosphorylase Pho1 from Barley

Released:

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1,4 glucan phosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 938 amino acids
Theoretical weight: 106.01 KDa
Source organism: Hordeum vulgare subsp. vulgare
Expression system: Escherichia coli
UniProt:
  • Canonical: F2E0G2 (Residues: 43-968; Coverage: 96%)
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 229.21Å b: 63.48Å c: 148.82Å
α: 90° β: 115.21° γ: 90°
R-values:
R R work R free
0.218 0.217 0.257
Expression system: Escherichia coli