Zinc in PDB 3zpc: Acinetobacter Baumannii Ribd, Form 1

All present enzymatic activity of Acinetobacter Baumannii Ribd, Form 1:
1.1.1.193; 3.5.4.26;

The structure of Acinetobacter Baumannii Ribd, Form 1, PDB code: 3zpc was solved by A.Dawson, P.Trumper, G.Chrysostomou, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	117.14 / 2.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	148.987, 189.555, 76.406, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 25

The binding sites of Zinc atom in the Acinetobacter Baumannii Ribd, Form 1 (pdb code 3zpc). 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 Baumannii Ribd, Form 1, PDB code: 3zpc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Acinetobacter Baumannii Ribd, Form 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Acinetobacter Baumannii Ribd, Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:27.8 occ:1.00 ND1 A:HIS54 2.1 27.9 1.0 SG A:CYS88 2.3 28.9 1.0 SG A:CYS79 2.3 27.1 1.0 O A:HOH2022 2.8 48.5 1.0 CB A:CYS88 3.0 24.8 1.0 CE1 A:HIS54 3.1 26.9 1.0 CG A:HIS54 3.1 28.2 1.0 CB A:CYS79 3.3 26.8 1.0 CB A:HIS54 3.5 28.6 1.0 N A:CYS79 3.6 28.2 1.0 N A:CYS88 3.9 29.8 1.0 OE2 A:GLU56 4.0 26.4 1.0 CA A:CYS88 4.0 27.5 1.0 CA A:CYS79 4.0 29.0 1.0 NE2 A:HIS54 4.2 29.3 1.0 OE1 A:GLU56 4.3 22.0 1.0 CD2 A:HIS54 4.3 28.7 1.0 CD A:GLU56 4.3 24.3 1.0 O A:HOH2028 4.4 24.9 1.0 O A:PRO86 4.7 38.5 1.0 C A:PRO78 4.8 28.5 1.0 O A:CYS79 4.8 30.4 1.0 C A:CYS79 4.8 30.4 1.0 O A:HOH2021 4.8 40.1 1.0 O A:HOH2023 4.8 39.1 1.0 C A:PRO87 5.0 35.8 1.0 CA A:HIS54 5.0 30.3 1.0

Zinc binding site 2 out of 2 in the Acinetobacter Baumannii Ribd, Form 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Acinetobacter Baumannii Ribd, Form 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:37.3 occ:1.00 ND1 B:HIS54 2.1 35.6 1.0 O B:HOH2016 2.3 37.9 1.0 SG B:CYS88 2.3 41.9 1.0 SG B:CYS79 2.4 39.8 1.0 CE1 B:HIS54 3.0 35.9 1.0 CG B:HIS54 3.1 38.6 1.0 CB B:CYS88 3.2 40.4 1.0 CB B:CYS79 3.4 35.0 1.0 CB B:HIS54 3.5 36.9 1.0 N B:CYS79 3.6 37.1 1.0 O B:HOH2019 3.7 44.4 1.0 N B:CYS88 3.8 39.2 1.0 OE2 B:GLU56 4.0 45.4 1.0 OE1 B:GLU56 4.1 46.2 1.0 CA B:CYS79 4.1 36.1 1.0 CA B:CYS88 4.1 40.9 1.0 NE2 B:HIS54 4.2 36.1 1.0 CD2 B:HIS54 4.3 38.5 1.0 O B:HOH2020 4.3 44.8 1.0 CD B:GLU56 4.3 46.4 1.0 O B:HOH2023 4.3 34.5 1.0 O B:PRO86 4.6 40.2 1.0 C B:PRO78 4.7 38.5 1.0 O B:CYS79 4.9 35.9 1.0 O B:HOH2015 4.9 33.7 1.0 CA B:PRO78 4.9 37.8 1.0 C B:CYS79 4.9 37.2 1.0 C B:PRO87 5.0 39.6 1.0

A.Dawson, P.Trumper, G.Chrysostomou, W.N.Hunter. Structure of Diaminohydroxyphosphoribosylaminopyrimidine Deaminase/5-Amino-6-(5-Phosphoribosylamino)Uracil Reductase From Acinetobacter Baumannii. Acta Crystallogr.,Sect.F V. 69 611 2013.
ISSN: ESSN 1744-3091
PubMed: 23722836
DOI: 10.1107/S174430911301292X