› 5w6j

X-ray diffraction
1.78Å resolution

Agrobacterium tumefaciens ADP-glucose pyrophosphorylase

Released:
DOI: 10.2210/pdb5w6j/pdb
PDB entry 5w6j coloured by chain, front view.
PDB entry 5w6j coloured by chain, side view.
PDB entry 5w6j coloured by chain, top view.
Source organism: Agrobacterium tumefaciens
Primary publication:
Structural analysis reveals a pyruvate-binding activator site in the Agrobacterium tumefaciens ADP-glucose pyrophosphorylase.
Hill BL, Mascarenhas R, Patel HP, Asencion Diez MD, Wu R, Iglesias AA, Liu D, Ballicora MA
J Biol Chem 294 1338-1348 (2019)
PMID: 30401744

Function and Biology Details

Reaction catalysed: 
ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphate adenylyltransferase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, T, U
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, T, U
Length: 420 amino acids
Theoretical weight: 47.1 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P39669 (Residues: 1-420; Coverage: 100%)
Gene name: glgC
Sequence domains: Nucleotidyl transferase

Ligands and Environments

1 bound ligand:
Ligand SO4 42 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 93.439Å b: 140.685Å c: 228.49Å
α: 72.04° β: 78.19° γ: 89.98°
R-values:
R R work R free
0.202 0.2 0.229
Expression system: Escherichia coli K-12

Quick links

Citations

1 review citation

Structure, function, and evolution of plant ADP-glucose pyrophosphorylase.
Figueroa et al. (2022)
2 other articles

3 mentions without citation

Structural analysis reveals a pyruvate-binding activator site in the Agrobacterium tumefaciens ADP-glucose pyrophosphorylase.
Hill et al. (2019)
2 more