› 3g2j

X-ray diffraction
2.14Å resolution

Crystal structure of 1-(beta-D-glucopyranosyl)-4-substituted-1,2,3-triazoles in complex with glycogen phosphorylase

Released:
DOI: 10.2210/pdb3g2j/pdb
PDB entry 3g2j coloured by chain, front view.
PDB entry 3g2j coloured by chain, side view.
PDB entry 3g2j coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Amide-1,2,3-triazole bioisosterism: the glycogen phosphorylase case
Chrysina ED, Bokor E, Alexacou K-M, Charavgi M-D, Oikonomakos GN, Zographos SE, Leonidas DD, Oikonomakos NG, Somsak L
Tetrahedron Asymmetry 20 733-740 (2009)

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 analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-132555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, muscle form Chain: A
Molecule details ›
Chain: A
Length: 842 amino acids
Theoretical weight: 97.52 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P00489 (Residues: 2-843; Coverage: 100%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
Ligand 9GP 1 x 9GP
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P43212
Unit cell:
a: 127.191Å b: 127.191Å c: 115.275Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.225

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