› 1z8d

X-ray diffraction
2.3Å resolution

Crystal Structure of Human Muscle Glycogen Phosphorylase a with AMP and Glucose

Released:
DOI: 10.2210/pdb1z8d/pdb
PDB entry 1z8d coloured by chain, front view.
PDB entry 1z8d coloured by chain, side view.
PDB entry 1z8d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of human muscle glycogen phosphorylase a with bound glucose and AMP: an intermediate conformation with T-state and R-state features.
Lukacs CM, Oikonomakos NG, Crowther RL, Hong LN, Kammlott RU, Levin W, Li S, Liu CM, Lucas-McGady D, Pietranico S, Reik L
Proteins 63 1123-6 (2006)
PMID: 16523484

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145714 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, muscle form Chain: A
Molecule details ›
Chain: A
Length: 842 amino acids
Theoretical weight: 97.53 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P11217 (Residues: 1-842; Coverage: 100%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

3 bound ligands:
Ligand GLC 1 x GLC
Ligand AMP 1 x AMP
Ligand ADE 1 x ADE
2 modified residues:
Ligand SEP 1 x SEP
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P21212
Unit cell:
a: 92.37Å b: 144Å c: 59.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.251
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

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

6 mentions without citation

Structural Basis for Allostery in PLP-dependent Enzymes.
Tran et al. (2022)
5 more