Zinc in PDB 2wt9: 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: 2wt9 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)	28.40 / 1.65
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	46.640, 46.890, 59.480, 113.19, 88.25, 115.61
R / Rfree (%)	17.9 / 23.5

The binding sites of Zinc atom in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease (pdb code 2wt9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease, PDB code: 2wt9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Acinetobacter Baumanii Nicotinamidase Pyrazinamidease within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1212 b:25.0 occ:1.00 O A:HOH2141 2.1 19.5 1.0 N A:NIO1216 2.2 21.1 1.0 OD2 A:ASP54 2.2 18.6 1.0 NE2 A:HIS56 2.3 15.7 1.0 O A:HOH2142 2.3 21.2 1.0 NE2 A:HIS89 2.3 19.9 1.0 C1 A:NIO1216 3.0 25.6 1.0 C5 A:NIO1216 3.1 21.3 1.0 CE1 A:HIS89 3.2 21.4 1.0 CG A:ASP54 3.2 16.8 1.0 CE1 A:HIS56 3.2 14.0 1.0 CD2 A:HIS56 3.2 20.3 1.0 CD2 A:HIS89 3.4 23.8 1.0 OD1 A:ASP54 3.4 20.7 1.0 OD1 A:ASP121 4.0 24.0 1.0 C2 A:NIO1216 4.3 21.5 1.0 ND1 A:HIS56 4.3 19.8 1.0 ND1 A:HIS89 4.3 18.9 1.0 CG A:HIS56 4.4 22.6 1.0 C4 A:NIO1216 4.4 20.9 1.0 CG A:HIS89 4.5 19.8 1.0 OG A:SER62 4.5 21.4 1.0 CB A:ASP54 4.5 21.4 1.0 CZ A:PHE21 4.6 25.6 1.0 OD2 A:ASP121 4.6 21.2 1.0 CG A:ASP121 4.7 20.7 1.0 C3 A:NIO1216 4.9 20.6 1.0 CE1 A:TYR123 4.9 25.2 1.0

Zinc binding site 2 out of 2 in the Acinetobacter Baumanii Nicotinamidase Pyrazinamidease


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Acinetobacter Baumanii Nicotinamidase Pyrazinamidease within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1212 b:24.4 occ:1.00 OD1 B:ASP54 2.1 18.6 1.0 NE2 B:HIS56 2.2 18.9 1.0 N B:NIO1216 2.2 17.0 1.0 NE2 B:HIS89 2.3 23.4 1.0 O B:HOH2149 2.3 16.8 1.0 O B:HOH2148 2.3 23.8 1.0 C5 B:NIO1216 3.0 22.2 1.0 CG B:ASP54 3.1 18.8 1.0 CE1 B:HIS89 3.1 18.7 1.0 CE1 B:HIS56 3.1 19.0 1.0 C1 B:NIO1216 3.1 27.8 1.0 CD2 B:HIS56 3.2 23.0 1.0 CD2 B:HIS89 3.3 20.6 1.0 OD2 B:ASP54 3.4 20.2 1.0 OD1 B:ASP121 4.0 21.8 1.0 ND1 B:HIS56 4.3 16.6 1.0 ND1 B:HIS89 4.3 17.1 1.0 CG B:HIS56 4.3 18.9 1.0 OG B:SER62 4.3 18.2 1.0 CB B:ASP54 4.4 20.9 1.0 C4 B:NIO1216 4.4 19.6 1.0 CG B:HIS89 4.4 20.8 1.0 C2 B:NIO1216 4.4 21.5 1.0 OD2 B:ASP121 4.6 20.9 1.0 CZ B:PHE21 4.6 20.9 1.0 CG B:ASP121 4.7 14.8 1.0 CE1 B:TYR123 4.9 20.8 1.0 C3 B:NIO1216 5.0 23.2 1.0 CD1 B:TYR123 5.0 23.6 1.0

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