Zinc in PDB 4lh8: Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli

All present enzymatic activity of Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli:
3.8.1.8;

The structure of Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli, PDB code: 4lh8 was solved by C.J.Jackson, C.W.Coppin, A.Alexandrov, M.Wilding, J.-W.Liu, J.Ubels, M.Paks, P.D.Carr, J.Newman, R.J.Russell, M.Field, M.Weik, J.G.Oakeshott, C.Scott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.78 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.091, 101.787, 79.890, 90.00, 103.24, 90.00
R / Rfree (%)	17.7 / 21.8

The binding sites of Zinc atom in the Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli (pdb code 4lh8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli, PDB code: 4lh8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:17.5 occ:0.78 O A:HOH626 2.1 19.9 1.0 NE2 A:HIS63 2.2 17.6 1.0 NE2 A:HIS238 2.2 19.5 1.0 NE2 A:HIS65 2.2 20.9 1.0 CE1 A:HIS63 3.1 21.9 1.0 CE1 A:HIS238 3.1 17.3 1.0 CE1 A:HIS65 3.2 22.7 1.0 CD2 A:HIS238 3.2 19.1 1.0 CD2 A:HIS65 3.2 19.7 1.0 CD2 A:HIS63 3.2 19.7 1.0 OE1 A:GLN129 4.2 22.0 1.0 ND1 A:HIS63 4.2 19.3 1.0 O A:HOH678 4.2 27.3 1.0 ND1 A:HIS238 4.3 22.6 1.0 NE2 A:HIS274 4.3 14.4 1.0 ND1 A:HIS65 4.3 22.3 1.0 CG A:HIS238 4.3 16.6 1.0 CG A:HIS63 4.3 17.0 1.0 CG A:HIS65 4.3 19.8 1.0 CG2 A:THR325 4.5 21.5 1.0 CB A:THR325 4.6 17.9 1.0 O A:HOH632 4.9 21.5 1.0 CD2 A:HIS274 5.0 16.9 1.0 O A:HOH972 5.0 37.6 1.0

Zinc binding site 2 out of 2 in the Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Triazine Hydrolase From Arthobacter Aurescens Modified For Maximum Expression in E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:24.6 occ:0.59 NE2 B:HIS63 2.0 24.1 1.0 O B:HOH681 2.2 26.0 1.0 CE1 B:HIS238 2.3 29.2 1.0 NE2 B:HIS65 2.5 28.4 1.0 CE1 B:HIS63 2.8 27.6 1.0 CE1 B:HIS65 3.0 30.9 1.0 NE2 B:HIS238 3.0 25.7 1.0 CD2 B:HIS63 3.2 31.3 1.0 ND1 B:HIS238 3.3 35.5 1.0 O B:HOH743 3.5 38.6 1.0 OE1 B:GLN129 3.6 23.9 0.5 CD2 B:HIS65 3.7 30.0 1.0 ND1 B:HIS63 4.0 29.7 1.0 CD B:GLN129 4.1 26.7 0.5 O B:HOH738 4.2 32.5 1.0 ND1 B:HIS65 4.2 32.9 1.0 CG B:HIS63 4.2 26.1 1.0 CD2 B:HIS238 4.2 25.3 1.0 OE1 B:GLN129 4.3 23.8 0.5 NE2 B:HIS274 4.3 17.8 1.0 CG B:HIS238 4.4 23.6 1.0 CG B:PRO131 4.5 28.3 0.5 NE2 B:GLN129 4.5 22.0 0.5 CG2 B:THR325 4.5 22.9 1.0 CG B:HIS65 4.6 25.3 1.0 CE2 B:PHE132 4.6 33.8 0.5 CB B:THR325 4.7 23.2 1.0 CG B:GLN129 4.9 25.0 0.5 CD2 B:HIS274 4.9 19.6 1.0 CZ B:PHE132 4.9 34.1 0.5

C.J.Jackson, C.W.Coppin, P.D.Carr, A.Aleksandrov, M.Wilding, E.Sugrue, J.Ubels, M.Paks, J.Newman, T.S.Peat, R.J.Russell, M.Field, M.Weik, J.G.Oakeshott, C.Scott. Apoenzyme Stabilization Results in 300-Fold Increased Soluble Production of the ZN2+-Dependent Dechlorinase Trzn. Appl.Environ.Microbiol. 2014.
ISSN: ESSN 1098-5336
PubMed: 24771025
DOI: 10.1128/AEM.00916-14