› 1l5s

X-ray diffraction
2.1Å resolution

Human liver glycogen phosphorylase complexed with uric acid, N-Acetyl-beta-D-glucopyranosylamine, and CP-403,700

Released:
DOI: 10.2210/pdb1l5s/pdb
PDB entry 1l5s coloured by chain, front view.
PDB entry 1l5s coloured by chain, side view.
PDB entry 1l5s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase.
Ekstrom JL, Pauly TA, Carty MD, Soeller WC, Culp J, Danley DE, Hoover DJ, Treadway JL, Gibbs EM, Fletterick RJ, Day YS, Myszka DG, Rath VL
Chem Biol 9 915-24 (2002)
PMID: 12204691

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-139195 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, liver form Chains: A, B
Molecule details ›
Chains: A, B
Length: 847 amino acids
Theoretical weight: 97.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06737 (Residues: 1-847; Coverage: 100%)
Gene name: PYGL
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
4 bound ligands:
Ligand NBG 2 x NBG
Ligand 700 2 x 700
Ligand URC 2 x URC
Ligand MRD 5 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P31
Unit cell:
a: 124.03Å b: 124.03Å c: 123.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 0.236
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
8 more