› 5huh

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + deamido-NAD(+) + NH(3) = AMP + diphosphate + NAD(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101810 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NH(3)-dependent NAD(+) synthetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 307 amino acids
Theoretical weight: 33.88 KDa
Source organism: Streptococcus pyogenes NZ131
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3BZ89 (Residues: 1-282; Coverage: 100%)
Gene names: Spy49_1281c, nadE
Sequence domains: NAD synthase
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
Ligand SO4 13 x SO4
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 49.521Å b: 93.104Å c: 128.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.226
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)