Zinc in PDB 3mpg: Dihydroorotase From Bacillus Anthracis

All present enzymatic activity of Dihydroorotase From Bacillus Anthracis:
3.5.2.3;

The structure of Dihydroorotase From Bacillus Anthracis, PDB code: 3mpg was solved by B.D.Santarsiero, S.Mehboob, M.E.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.360, 80.784, 104.772, 90.00, 100.21, 90.00
R / Rfree (%)	21.2 / 29.3

The binding sites of Zinc atom in the Dihydroorotase From Bacillus Anthracis (pdb code 3mpg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Dihydroorotase From Bacillus Anthracis, PDB code: 3mpg:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Dihydroorotase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dihydroorotase From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn429 b:45.8 occ:1.00 NE2 A:HIS59 2.2 29.6 1.0 OD2 A:ASP304 2.4 41.4 1.0 NE2 A:HIS61 2.4 37.1 1.0 OD2 A:ASP151 2.5 52.5 1.0 CD2 A:HIS59 3.2 28.4 1.0 CE1 A:HIS59 3.2 29.3 1.0 CD2 A:HIS61 3.3 35.8 1.0 CG A:ASP151 3.3 53.1 1.0 ZN A:ZN430 3.3 53.5 1.0 OD1 A:ASP151 3.4 51.9 1.0 CG A:ASP304 3.4 38.2 1.0 CE1 A:HIS61 3.4 36.2 1.0 OD1 A:ASP304 3.8 39.8 1.0 ND1 A:HIS59 4.3 29.7 1.0 CG A:HIS59 4.3 30.2 1.0 NE2 A:HIS231 4.4 38.0 1.0 CG A:HIS61 4.5 34.6 1.0 ND1 A:HIS61 4.5 37.2 1.0 CD2 A:HIS231 4.5 36.6 1.0 CG A:MET91 4.5 40.3 1.0 CB A:ASP304 4.6 36.9 1.0 CB A:ASP151 4.7 53.9 1.0 O A:HOH484 4.9 33.6 1.0 CA A:ASP304 4.9 37.5 1.0

Zinc binding site 2 out of 4 in the Dihydroorotase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Dihydroorotase From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn430 b:53.5 occ:1.00 NE2 A:HIS231 2.4 38.0 1.0 ND1 A:HIS178 2.4 46.5 1.0 OD1 A:ASP151 2.5 51.9 1.0 CE1 A:HIS178 3.0 45.5 1.0 CE1 A:HIS231 3.2 32.4 1.0 ZN A:ZN429 3.3 45.8 1.0 CG A:ASP151 3.4 53.1 1.0 CG A:HIS178 3.4 44.2 1.0 CD2 A:HIS231 3.5 36.6 1.0 OD2 A:ASP151 3.7 52.5 1.0 N A:GLY152 3.8 57.4 1.0 CB A:HIS178 4.0 42.1 1.0 NE2 A:HIS178 4.1 46.2 1.0 CE1 A:HIS59 4.1 29.3 1.0 NE2 A:HIS59 4.2 29.6 1.0 O A:ASN277 4.3 38.9 1.0 CD2 A:HIS178 4.3 43.8 1.0 CA A:GLY152 4.4 56.3 1.0 ND1 A:HIS231 4.4 37.4 1.0 CG A:HIS231 4.6 35.9 1.0 CB A:ASP151 4.6 53.9 1.0 C A:ASP151 4.7 56.5 1.0 CA A:HIS178 4.8 41.4 1.0 CA A:ASP151 4.8 54.9 1.0 OD2 A:ASP304 4.9 41.4 1.0 OD1 A:ASP304 4.9 39.8 1.0

Zinc binding site 3 out of 4 in the Dihydroorotase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Dihydroorotase From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn429 b:55.0 occ:1.00 NE2 B:HIS61 2.2 58.3 1.0 NE2 B:HIS59 2.3 42.0 1.0 OD2 B:ASP151 2.4 61.5 1.0 OD2 B:ASP304 2.7 49.4 1.0 CE1 B:HIS59 3.0 44.5 1.0 CE1 B:HIS61 3.1 57.9 1.0 CD2 B:HIS61 3.3 58.4 1.0 CG B:ASP151 3.3 59.5 1.0 ZN B:ZN430 3.3 53.0 1.0 CG B:ASP304 3.3 48.4 1.0 CD2 B:HIS59 3.4 44.5 1.0 OD1 B:ASP304 3.4 49.2 1.0 OD1 B:ASP151 3.4 59.6 1.0 O B:HOH494 4.0 42.0 1.0 ND1 B:HIS59 4.2 44.3 1.0 ND1 B:HIS61 4.2 58.2 1.0 CG B:HIS61 4.3 57.8 1.0 CG B:HIS59 4.4 43.0 1.0 CG B:MET91 4.4 49.7 1.0 NE2 B:HIS231 4.5 46.7 1.0 CD2 B:HIS231 4.6 44.4 1.0 CB B:ASP304 4.6 45.2 1.0 CB B:ASP151 4.7 58.4 1.0

Zinc binding site 4 out of 4 in the Dihydroorotase From Bacillus Anthracis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Dihydroorotase From Bacillus Anthracis within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn430 b:53.0 occ:1.00 NE2 B:HIS231 2.4 46.7 1.0 ND1 B:HIS178 2.5 46.4 1.0 OD1 B:ASP151 2.6 59.6 1.0 CE1 B:HIS178 3.2 47.0 1.0 CE1 B:HIS231 3.3 44.9 1.0 ZN B:ZN429 3.3 55.0 1.0 CG B:ASP151 3.4 59.5 1.0 CD2 B:HIS231 3.4 44.4 1.0 O B:HOH494 3.4 42.0 1.0 CG B:HIS178 3.5 44.5 1.0 OD2 B:ASP151 3.7 61.5 1.0 CB B:HIS178 3.9 42.4 1.0 N B:GLY152 3.9 56.2 1.0 CE1 B:HIS59 4.0 44.5 1.0 NE2 B:HIS178 4.3 45.2 1.0 NE2 B:HIS59 4.3 42.0 1.0 ND1 B:HIS231 4.4 46.4 1.0 CD2 B:HIS178 4.4 44.7 1.0 CA B:GLY152 4.4 55.3 1.0 O B:ASN277 4.5 43.5 1.0 OD1 B:ASP304 4.5 49.2 1.0 CG B:HIS231 4.5 44.5 1.0 CA B:HIS178 4.6 41.7 1.0 CB B:ASP151 4.7 58.4 1.0 C B:ASP151 4.8 56.3 1.0 CA B:ASP151 4.8 56.4 1.0 CB B:CYS230 4.9 41.0 1.0

S.Mehboob, D.C.Mulhearn, K.Truong, M.E.Johnson, B.D.Santarsiero. Structure of Dihydroorotase From Bacillus Anthracis at 2.6A Resolution. Acta Crystallogr.,Sect.F V. 66 1432 2010.
ISSN: ESSN 1744-3091
PubMed: 21045288
DOI: 10.1107/S1744309110037085