› 5huo

X-ray diffraction
2.8Å 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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197524 (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: 314 amino acids
Theoretical weight: 34.43 KDa
Source organism: Streptococcus pyogenes GA06023
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: U2UIT5 (Residues: 1-290; Coverage: 100%)
Gene names: HMPREF1231_0804, nadC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 20 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2221
Unit cell:
a: 106.203Å b: 186.261Å c: 221.906Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.255
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)