› 3mmx

X-ray diffraction
2.55Å resolution

Bacillus anthracis NadD (baNadD) in complex with compound 1_02_3

Released:
DOI: 10.2210/pdb3mmx/pdb
PDB entry 3mmx coloured by chain, front view.
PDB entry 3mmx coloured by chain, side view.
PDB entry 3mmx coloured by chain, top view.
Source organism: Bacillus anthracis
Primary publication:
Complexes of bacterial nicotinate mononucleotide adenylyltransferase with inhibitors: implication for structure-based drug design and improvement.
Huang N, Kolhatkar R, Eyobo Y, Sorci L, Rodionova I, Osterman AL, Mackerell AD, Zhang H
J Med Chem 53 5229-39 (2010)
PMID: 20578699

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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable nicotinate-nucleotide adenylyltransferase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
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

4 bound ligands:
Ligand K 9 x K
Ligand CIT 8 x CIT
Ligand KJZ 2 x KJZ
Ligand DMS 4 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 295.151Å b: 46.446Å c: 114.952Å
α: 90° β: 91.42° γ: 90°
R-values:
R R work R free
0.223 0.221 0.263
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Reproducing crystal binding modes of ligand functional groups using Site-Identification by Ligand Competitive Saturation (SILCS) simulations.
Raman et al. (2011)
1 more