5lra

X-ray diffraction
3Å resolution

Plastidial phosphorylase PhoI from barley in complex with maltotetraose

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-514307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
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
Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer : NEW Components: GLC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: C2
Unit cell:
a: 227.69Å b: 63.15Å c: 148.19Å
α: 90° β: 114.72° γ: 90°
R-values:
R R work R free
0.196 0.195 0.243
Expression system: Escherichia coli