› 3mla

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-111162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable nicotinate-nucleotide adenylyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 191 amino acids
Theoretical weight: 22.11 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: C3L5T6 (Residues: 1-189; Coverage: 100%)
Gene names: BAMEG_4595, nadD
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

3 bound ligands:
Ligand JJZ 1 x JJZ
Ligand FMT 5 x FMT
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 88.586Å b: 97.498Å c: 44.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.23
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The Prospective Synergy of Antitubercular Drugs With NAD Biosynthesis Inhibitors.
Rohde et al. (2020)
12 other articles

3 mentions without citation

New developments in vaccines, inhibitors of anthrax toxins, and antibiotic therapeutics for Bacillus anthracis.
Beierlein et al. (2011)
2 more