› 2f3u

X-ray diffraction
1.93Å resolution

Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)-N'-cyclopropyl oxalamide complex

Released:
DOI: 10.2210/pdb2f3u/pdb
PDB entry 2f3u coloured by chain, front view.
PDB entry 2f3u coloured by chain, side view.
PDB entry 2f3u coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Binding of oxalyl derivatives of beta-d-glucopyranosylamine to muscle glycogen phosphorylase b.
Hadjiloi T, Tiraidis C, Chrysina ED, Leonidas DD, Oikonomakos NG, Tsipos P, Gimisis T
Bioorg Med Chem 14 3872-82 (2006)
PMID: 16464598

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-132556 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, muscle form Chain: A
Molecule details ›
Chain: A
Length: 842 amino acids
Theoretical weight: 97.29 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


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand 8GP 1 x 8GP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P43212
Unit cell:
a: 127.957Å b: 127.957Å c: 116.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.191 0.21

Quick links

Citations

1 review citation

Glycogen phosphorylase inhibitors: a patent review (2008 - 2012).
Gaboriaud-Kolar et al. (2013)
5 other articles