Arsenic in PDB 2wta: Acinetobacter Baumanii Nicotinamidase Pyrazinamidease

All present enzymatic activity of Acinetobacter Baumanii Nicotinamidase Pyrazinamidease:
3.5.1.19;

The structure of Acinetobacter Baumanii Nicotinamidase Pyrazinamidease, PDB code: 2wta was solved by P.K.Fyfe, V.A.Rao, A.Zemla, S.Cameron, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.54 / 1.70
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	50.688, 46.507, 107.602, 90.00, 101.97, 90.00
R / Rfree (%)	14.748 / 17.661

The structure of Acinetobacter Baumanii Nicotinamidase Pyrazinamidease also contains other interesting chemical elements:

Chlorine	(Cl)	3 atoms
Zinc	(Zn)	1 atom

The binding sites of Arsenic atom in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease (pdb code 2wta). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease, PDB code: 2wta:

Arsenic binding site 1 out of 1 in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Acinetobacter Baumanii Nicotinamidase Pyrazinamidease within 5.0Å range: probe atom residue distance (Å) B Occ A:As159 b:22.5 occ:0.20 AS A:CAF159 0.0 22.5 0.2 C2 A:VGL1216 0.5 30.5 0.8 O2 A:VGL1216 0.8 28.4 0.8 O1 A:VGL1216 1.6 34.6 0.8 O1 A:CAF159 1.7 20.3 0.2 C1 A:VGL1216 1.8 26.9 0.8 CE1 A:CAF159 2.0 21.0 0.2 CE2 A:CAF159 2.0 20.9 0.2 SG A:CAF159 2.2 18.1 0.2 SG A:CAF159 2.4 19.0 0.8 N2 A:VGL1216 2.6 28.4 0.8 C6 A:VGL1216 2.9 26.3 0.8 CB A:CAF159 3.0 14.8 0.8 CB A:CAF159 3.1 15.4 0.2 N A:CAF159 3.3 15.2 0.2 N A:CAF159 3.3 14.8 0.8 N A:ALA155 3.5 13.3 1.0 CA A:CAF159 3.7 15.2 0.2 CA A:CAF159 3.7 14.8 0.8 O A:ILE154 3.8 13.6 1.0 C3 A:VGL1216 3.9 25.6 0.8 CB A:PHE158 4.0 15.5 1.0 C A:ILE154 4.1 11.8 1.0 N5 A:VGL1216 4.1 22.6 0.8 OD1 A:ASP16 4.2 21.6 1.0 CB A:ALA155 4.3 12.7 1.0 C A:PHE158 4.4 15.3 1.0 CA A:ALA155 4.5 12.8 1.0 C4 A:VGL1216 4.5 25.6 0.8 CZ A:PHE21 4.7 19.1 1.0 CA A:PHE158 4.7 15.5 1.0 O A:ALA155 4.8 13.8 1.0 CE1 A:PHE21 4.8 20.6 1.0 CD1 A:TYR123 4.8 18.1 1.0 C A:CAF159 5.0 14.4 0.2 C A:CAF159 5.0 13.9 0.8

P.K.Fyfe, V.A.Rao, A.Zemla, S.Cameron, W.N.Hunter. Specificity and Mechanism of Acinetobacter Baumanii Nicotinamidase: Implications For Activation of the Front-Line Tuberculosis Drug Pyrazinamide. Angew.Chem.Int.Ed.Engl. V. 48 9176 2009.
ISSN: ISSN 1433-7851
PubMed: 19859929
DOI: 10.1002/ANIE.200903407