› 6v96

X-ray diffraction
1.8Å resolution

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-186507 (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, V
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, T, V
Length: 440 amino acids
Theoretical weight: 49.31 KDa
Source organism: Agrobacterium fabrum str. C58
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8U8L5 (Residues: 1-420; Coverage: 100%)
Gene names: AGR_L_1560, Atu4076, glgC
Sequence domains: Nucleotidyl transferase

Ligands and Environments

2 bound ligands:
Ligand CIT 20 x CIT
Ligand GOL 22 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P1
Unit cell:
a: 93.607Å b: 141.187Å c: 229.427Å
α: 107.926° β: 101.725° γ: 89.97°
R-values:
R R work R free
0.195 0.193 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Site-directed mutagenesis of Serine-72 reveals the location of the fructose 6-phosphate regulatory site of the Agrobacterium tumefaciens ADP-glucose pyrophosphorylase.
Alghamdi et al. (2022)