Zinc in PDB 3hyp: Crystal Structure of Bacteroides Fragilis TRXP_S105G Mutant

The structure of Crystal Structure of Bacteroides Fragilis TRXP_S105G Mutant, PDB code: 3hyp 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)	29.89 / 2.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.506, 94.506, 82.539, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 26.3

The binding sites of Zinc atom in the Crystal Structure of Bacteroides Fragilis TRXP_S105G Mutant (pdb code 3hyp). 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_S105G Mutant, PDB code: 3hyp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Bacteroides Fragilis TRXP_S105G Mutant


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_S105G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn142 b:34.4 occ:1.00 OD2 A:ASP100 2.0 34.4 1.0 OE2 B:GLU40 2.0 36.4 1.0 OE2 A:GLU96 2.1 34.1 1.0 CG A:ASP100 2.8 34.0 1.0 CD B:GLU40 2.8 36.3 1.0 CD A:GLU96 2.9 37.2 1.0 OD1 A:ASP100 3.0 31.4 1.0 OE1 B:GLU40 3.0 39.2 1.0 CG A:GLU96 3.2 37.4 1.0 OH B:TYR39 3.6 32.9 1.0 OE1 A:GLU96 4.1 35.5 1.0 CB A:ASP100 4.2 37.7 1.0 NH2 B:ARG29 4.2 33.7 1.0 CG B:GLU40 4.3 35.7 1.0 CE1 B:TYR39 4.4 38.0 1.0 O A:HOH144 4.4 39.8 1.0 CZ B:TYR39 4.4 36.3 1.0 NE B:ARG29 4.6 33.9 1.0 CB A:GLU96 4.7 40.0 1.0 CZ B:ARG29 4.8 33.8 1.0 O A:GLU96 5.0 36.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Bacteroides Fragilis TRXP_S105G Mutant


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_S105G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn142 b:33.4 occ:1.00 OD2 B:ASP100 2.1 35.0 1.0 OE1 A:GLU40 2.2 34.8 1.0 OE2 A:GLU40 2.4 32.4 1.0 CD A:GLU40 2.6 31.6 1.0 CG B:ASP100 2.8 37.4 1.0 OD1 B:ASP100 2.8 37.8 1.0 OE2 B:GLU96 3.5 35.1 1.0 OH A:TYR39 4.0 35.0 1.0 CG A:GLU40 4.1 35.0 1.0 CB B:ASP100 4.2 34.6 1.0 CD B:GLU96 4.3 35.8 1.0 CG B:GLU96 4.3 34.9 1.0 CE2 A:TYR39 4.4 37.8 1.0 O B:HOH145 4.5 42.2 1.0 CZ A:TYR39 4.6 35.9 1.0 NH2 A:ARG29 4.7 35.5 1.0 O B:HOH169 5.0 40.9 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