› 2azd

X-ray diffraction
2.16Å resolution

X-Ray studies on Maltodextrin Phosphorylase (MalP) Complexes: recognition of substrates and CATALYTIC mechanism of phosphorylase family

Released:
DOI: 10.2210/pdb2azd/pdb
PDB entry 2azd coloured by chain, front view.
PDB entry 2azd coloured by chain, side view.
PDB entry 2azd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
X-ray studies on ternary complexes of maltodextrin phosphorylase.
Campagnolo M, Campa C, Zorzi RD, Wuerges J, Geremia S
Arch Biochem Biophys 471 11-9 (2008)
PMID: 18164678

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-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: BGC, GLC
Carbohydrate polymer
2 bound ligands:
Ligand VO4 2 x VO4
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 76.779Å b: 105.892Å c: 220.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.25
Expression system: Escherichia coli

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Citations

1 review citation

Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.
Li et al. (2022)
3 other articles