Zinc in PDB 7qul: Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant

All present enzymatic activity of Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant:
1.1.1.368;

The structure of Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant, PDB code: 7qul was solved by M.L.Petchey, F.Stark, M.Ansorge-Schumacher, G.Grogan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.47 / 1.80
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	51.625, 72.892, 81.276, 90, 103.59, 90
R / Rfree (%)	21.2 / 27.4

The binding sites of Zinc atom in the Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant (pdb code 7qul). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant, PDB code: 7qul:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:16.6 occ:1.00 SG A:CYS97 2.3 20.2 1.0 SG A:CYS94 2.3 22.9 1.0 SG A:CYS100 2.3 19.2 1.0 SG A:CYS108 2.4 15.2 1.0 CB A:CYS97 3.2 24.3 1.0 CB A:CYS94 3.3 22.2 1.0 CB A:CYS108 3.3 18.6 1.0 N A:CYS94 3.5 20.4 1.0 CB A:CYS100 3.5 27.1 1.0 CA A:CYS94 3.8 23.3 1.0 N A:GLY95 3.8 26.2 1.0 N A:CYS97 3.9 27.9 1.0 CA A:CYS97 4.0 28.9 1.0 O A:HOH691 4.1 22.9 1.0 N A:CYS100 4.1 35.1 1.0 C A:CYS94 4.2 25.7 1.0 CA A:CYS108 4.3 21.6 1.0 CA A:CYS100 4.4 30.4 1.0 C A:PRO93 4.5 19.8 1.0 O A:CYS97 4.6 33.1 1.0 C A:CYS97 4.6 31.5 1.0 N A:THR96 4.6 31.1 1.0 CB A:PRO93 4.9 18.1 1.0 CA A:GLY95 4.9 30.3 1.0 C A:CYS108 5.0 21.0 1.0

Zinc binding site 2 out of 2 in the Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alcohol Dehydrogenase From Thauera Aromatica K319A/K320A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:14.5 occ:1.00 OE2 A:GLU66 1.8 9.9 1.0 OD2 A:ASP156 2.0 13.8 1.0 NE2 A:HIS65 2.0 13.1 1.0 SG A:CYS42 2.3 14.8 1.0 CD A:GLU66 3.0 10.3 1.0 CG A:ASP156 3.0 14.0 1.0 CB A:CYS42 3.0 14.9 1.0 CE1 A:HIS65 3.0 13.7 1.0 CD2 A:HIS65 3.0 12.7 1.0 CB A:ASP156 3.3 12.6 1.0 CG A:GLU66 3.5 10.3 1.0 O A:HOH601 3.7 21.4 1.0 NH2 A:ARG350 3.9 15.8 1.0 OE1 A:GLU66 4.1 10.7 1.0 ND1 A:HIS65 4.1 14.2 1.0 CG A:HIS65 4.1 12.4 1.0 OD1 A:ASP156 4.1 14.5 1.0 CA A:CYS42 4.4 15.6 1.0 O A:HOH571 4.7 12.1 1.0 OG1 A:THR44 4.8 15.5 1.0 CA A:ASP156 4.8 12.3 1.0 CB A:THR44 4.8 14.9 1.0

F.Stark, C.Loderer, M.Petchey, G.Grogan, M.B.Ansorge-Schumacher. Advanced Insights Into Catalytic and Structural Features of the Zinc-Dependent Alcohol Dehydrogenase From Thauera Aromatica. Chembiochem V. 23 00149 2022.
ISSN: ESSN 1439-7633
PubMed: 35557486
DOI: 10.1002/CBIC.202200149