1zcv

X-ray diffraction
1.98Å resolution

apo form of a mutant of glycogenin in which Asp159 is replaced by Asn

Released:
Source organism: Oryctolagus cuniculus
Primary publication:
Requirements for catalysis in mammalian glycogenin.
J Biol Chem 280 23892-9 (2005)
PMID: 15849187

Function and Biology Details

Reaction catalysed:
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogenin-1 Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 39.6 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P13280 (Residues: 1-333; Coverage: 100%)
Gene names: GYG, GYG1
Sequence domains: Glycosyl transferase family 8
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: I222
Unit cell:
a: 59.03Å b: 105.78Å c: 122.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.209 0.218
Expression system: Escherichia coli BL21