› 1ggn

X-ray diffraction
2.36Å resolution

Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design

Released:
DOI: 10.2210/pdb1ggn/pdb
PDB entry 1ggn coloured by chain, front view.
PDB entry 1ggn coloured by chain, side view.
PDB entry 1ggn coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Kinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase B.
Oikonomakos NG, Skamnaki VT, Osz E, Szilágyi L, Somsák L, Docsa T, Tóth B, Gergely P
Bioorg Med Chem 10 261-8 (2002)
PMID: 11741774

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-523539 (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 GLS 1 x GLS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P43212
Unit cell:
a: 128.5Å b: 128.5Å c: 116.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.233

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Citations

1 review citation

Structural glycobiology: a game of snakes and ladders.
DeMarco et al. (2008)
26 other articles