1l5w

X-ray diffraction
1.8Å resolution

Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and 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:

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: 90.55 KDa
Source organism: Escherichia coli
Expression system: 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: GLC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 74.508Å b: 105.236Å c: 217.361Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.216
Expression system: Escherichia coli