› 3g2h

X-ray diffraction
2.03Å resolution

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

Released:
DOI: 10.2210/pdb3g2h/pdb
PDB 3g2h coloured by chain and viewed from the front.
PDB 3g2h coloured by chain and viewed from the side.
PDB 3g2h coloured by chain and viewed from the top.
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
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

3 bound ligands:
Ligand KOT 1 x KOT
Ligand DMS 1 x DMS
Ligand IMP 1 x IMP
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: 127.287Å b: 127.287Å c: 115.615Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.22

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