› 1abb

X-ray diffraction
2.8Å resolution

CONTROL OF PHOSPHORYLASE B CONFORMATION BY A MODIFIED COFACTOR: CRYSTALLOGRAPHIC STUDIES ON R-STATE GLYCOGEN PHOSPHORYLASE RECONSTITUTED WITH PYRIDOXAL 5'-DIPHOSPHATE

Released:
DOI: 10.2210/pdb1abb/pdb
PDB entry 1abb coloured by chain, front view.
PDB entry 1abb coloured by chain, side view.
PDB entry 1abb coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Control of phosphorylase b conformation by a modified cofactor: crystallographic studies on R-state glycogen phosphorylase reconstituted with pyridoxal 5'-diphosphate.
Leonidas DD, Oikonomakos NG, Papageorgiou AC, Acharya KR, Barford D, Johnson LN
Protein Sci 1 1112-22 (1992)
PMID: 1304390

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132557 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, muscle form Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 828 amino acids
Theoretical weight: 95.66 KDa
Source organism: Oryctolagus cuniculus
Expression system: Not provided
UniProt:
  • Canonical: P00489 (Residues: 11-838; Coverage: 98%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PDP 4 x PDP
2 bound ligands:
Ligand SO4 4 x SO4
Ligand IMP 4 x IMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 119Å b: 188.1Å c: 88.1Å
α: 90° β: 109.29° γ: 90°
R-values:
R R work R free
0.21 0.21 not available
Expression system: Not provided

Quick links

Citations

1 review citation

Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers.
Harrus et al. (2018)
8 other articles

2 mentions without citation

An atlas of substrate specificities for the human serine/threonine kinome.
Johnson et al. (2023)
1 more