Zinc in PDB 8eiw: Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide

All present enzymatic activity of Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide:
1.1.1.1;

The structure of Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide, PDB code: 8eiw was solved by C.Zheng, I.I.Mathews, S.G.Boxer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.12 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.96, 71.64, 92.68, 90, 102.98, 90
R / Rfree (%)	17.8 / 20.4

The structure of Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide also contains other interesting chemical elements:

Cobalt

(Co)

2 atoms

The binding sites of Zinc atom in the Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide (pdb code 8eiw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide, PDB code: 8eiw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:25.2 occ:1.00 SG A:CYS103 2.2 24.1 1.0 SG A:CYS111 2.3 23.6 1.0 SG A:CYS100 2.3 24.1 1.0 SG A:CYS97 2.4 26.3 1.0 CB A:CYS111 3.4 25.4 1.0 CB A:CYS100 3.4 26.6 1.0 CB A:CYS97 3.4 24.3 1.0 CB A:CYS103 3.4 25.0 1.0 N A:CYS97 3.5 24.3 1.0 CA A:CYS111 3.8 23.2 1.0 N A:CYS100 3.8 27.9 1.0 CA A:CYS97 3.9 23.7 1.0 N A:LEU112 3.9 22.7 1.0 N A:GLY98 3.9 26.9 1.0 CA A:CYS100 4.2 28.7 1.0 N A:CYS103 4.2 22.9 1.0 C A:CYS111 4.3 23.4 1.0 C A:CYS97 4.3 31.1 1.0 CA A:CYS103 4.4 24.3 1.0 N A:LYS99 4.5 28.9 1.0 C A:GLN96 4.6 22.8 1.0 CG A:LYS113 4.7 29.9 1.0 N A:LYS113 4.8 24.6 1.0 C A:CYS100 4.9 27.4 1.0 CA A:GLN96 4.9 21.1 1.0 CA A:GLY98 4.9 30.5 1.0 O A:CYS100 5.0 27.5 1.0

Zinc binding site 2 out of 2 in the Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase in Complex with Nadh and N-Cyclohexylformamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:23.9 occ:1.00 SG B:CYS111 2.3 22.9 1.0 SG B:CYS103 2.4 23.2 1.0 SG B:CYS97 2.4 23.7 1.0 SG B:CYS100 2.4 24.4 1.0 CB B:CYS100 3.4 25.6 1.0 CB B:CYS111 3.4 20.5 1.0 CB B:CYS103 3.4 25.1 1.0 CB B:CYS97 3.4 26.3 1.0 N B:CYS97 3.5 24.0 1.0 N B:CYS100 3.8 24.7 1.0 CA B:CYS111 3.8 22.8 1.0 CA B:CYS97 3.9 26.1 1.0 N B:GLY98 3.9 26.1 1.0 N B:LEU112 4.0 21.0 1.0 CA B:CYS100 4.2 27.9 1.0 N B:CYS103 4.2 20.3 1.0 C B:CYS97 4.3 27.6 1.0 C B:CYS111 4.3 19.8 1.0 CA B:CYS103 4.4 22.0 1.0 N B:LYS99 4.4 25.5 1.0 C B:GLN96 4.6 25.5 1.0 CG B:LYS113 4.8 26.3 1.0 C B:CYS100 4.9 25.4 1.0 N B:LYS113 4.9 21.9 1.0 CA B:GLY98 4.9 27.1 1.0 CA B:GLN96 4.9 21.6 1.0 C B:LYS99 5.0 29.7 1.0 O B:CYS100 5.0 25.6 1.0

C.Zheng, I.I.Mathews, S.G.Boxer. Structure of Cobalt(II)-Substituted Horse Liver Alcohol Dehydrogenase at 1.65 Angstroms Resolution To Be Published.