Zinc in PDB 3hxs: Crystal Structure of Bacteroides Fragilis Trxp

The structure of Crystal Structure of Bacteroides Fragilis Trxp, PDB code: 3hxs was solved by S.R.Shouldice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.71 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.568, 94.568, 82.518, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23.7

The binding sites of Zinc atom in the Crystal Structure of Bacteroides Fragilis Trxp (pdb code 3hxs). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Bacteroides Fragilis Trxp, PDB code: 3hxs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Bacteroides Fragilis Trxp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Bacteroides Fragilis Trxp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn142 b:26.5 occ:1.00 OE2 A:GLU40 2.0 26.1 1.0 O B:HOH211 2.1 23.2 1.0 OD2 B:ASP100 2.1 23.4 1.0 CD A:GLU40 2.7 29.2 1.0 OE1 A:GLU40 2.8 27.5 1.0 CG B:ASP100 2.8 21.5 1.0 OD1 B:ASP100 3.0 25.9 1.0 OE2 B:GLU96 3.7 27.6 1.0 OH A:TYR39 3.9 27.2 1.0 CE2 A:TYR39 4.1 24.5 1.0 CG A:GLU40 4.2 18.8 1.0 CB B:ASP100 4.2 19.8 1.0 CZ A:TYR39 4.5 23.5 1.0 CG B:GLU96 4.5 29.7 1.0 CD B:GLU96 4.5 33.6 1.0 NH2 A:ARG29 4.7 26.4 1.0 O B:HOH226 5.0 43.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Bacteroides Fragilis Trxp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Bacteroides Fragilis Trxp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn143 b:25.7 occ:1.00 OD2 A:ASP100 1.9 27.8 1.0 OE2 B:GLU40 1.9 24.3 1.0 OE2 A:GLU96 2.1 25.2 1.0 CG A:ASP100 2.8 22.8 1.0 CD B:GLU40 2.9 33.8 1.0 OD1 A:ASP100 3.0 26.6 1.0 CD A:GLU96 3.1 27.8 1.0 OE1 B:GLU40 3.1 26.3 1.0 CG A:GLU96 3.3 25.1 1.0 OH B:TYR39 3.7 21.9 1.0 NH2 B:ARG29 4.1 24.7 1.0 CB A:ASP100 4.2 22.5 1.0 OE1 A:GLU96 4.2 25.5 1.0 CG B:GLU40 4.3 26.9 1.0 O A:HOH170 4.5 38.1 1.0 CZ B:TYR39 4.5 22.9 1.0 NE B:ARG29 4.5 29.5 1.0 CE1 B:TYR39 4.5 17.7 1.0 CZ B:ARG29 4.7 25.6 1.0 CB A:GLU96 4.8 29.4 1.0 O A:GLU96 4.8 22.8 1.0

S.R.Shouldice, S.H.Cho, D.Boyd, B.Heras, M.Eser, J.Beckwith, P.Riggs, J.L.Martin, M.Berkmen. In Vivo Oxidative Protein Folding Can Be Facilitated By Oxidation-Reduction Cycling Mol.Microbiol. V. 75 13 2010.
ISSN: ISSN 0950-382X
PubMed: 19968787
DOI: 10.1111/J.1365-2958.2009.06952.X