› 5hup

X-ray diffraction
3.42Å resolution

Function and Biology Details

Reaction catalysed: 
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172901 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
nicotinate-nucleotide diphosphorylase (carboxylating) Chains: A, B, C, E, F, H
Molecule details ›
Chains: A, B, C, E, F, H
Length: 315 amino acids
Theoretical weight: 34.5 KDa
Source organism: Streptococcus pyogenes MGAS10750
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q1J647 (Residues: 10-299; Coverage: 97%)
Gene names: MGAS10750_Spy1186, nadC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 17 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2221
Unit cell:
a: 108.149Å b: 188.816Å c: 222.181Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.233 0.294
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

A structural perspective on the PP-loop ATP pyrophosphatase family.
Fellner et al. (2018)
1 other article

1 mention without citation

Streptococcus pyogenes quinolinate-salvage pathway-structural and functional studies of quinolinate phosphoribosyl transferase and NH3 -dependent NAD+ synthetase.
Booth et al. (2017)