1e4o

X-ray diffraction
2.9Å resolution

Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question

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:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-132558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltodextrin phosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 796 amino acids
Theoretical weight: 90.5 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P00490 (Residues: 2-797; Coverage: 100%)
Gene names: JW5689, b3417, malP
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
Carbohydrate polymer : NEW Components: BGC, GLC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P212121
Unit cell:
a: 74.45Å b: 105.69Å c: 214.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.245 0.306