› 2gpb

X-ray diffraction
2.3Å resolution

COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B

Released:
DOI: 10.2210/pdb2gpb/pdb
PDB entry 2gpb coloured by chain, front view.
PDB entry 2gpb coloured by chain, side view.
PDB entry 2gpb coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Comparison of the binding of glucose and glucose 1-phosphate derivatives to T-state glycogen phosphorylase b.
Martin JL, Johnson LN, Withers SG
Biochemistry 29 10745-57 (1990)
PMID: 2125493

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
Expression system: Not provided
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 GLC 1 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
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
0.181 0.181 not available
Expression system: Not provided

Quick links

Citations

7 review citations

Phosphorylase: a biological transducer.
Browner et al. (1992)
6 more

5 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
4 more