Zinc in PDB 8g2x: Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole

All present enzymatic activity of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole, PDB code: 8g2x was solved by B.V.Plapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 1.47
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	44.13, 50.8, 92.41, 92.09, 102.96, 109.68
R / Rfree (%)	17.3 / 19.1

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole (pdb code 8g2x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole, PDB code: 8g2x:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:13.9 occ:1.00 NE2 A:HIS67 2.1 10.7 1.0 N1 A:PZO404 2.1 11.0 1.0 SG A:CYS174 2.3 13.4 1.0 SG A:CYS46 2.3 14.0 1.0 CD2 A:HIS67 3.0 12.1 1.0 C5N A:NAJ403 3.1 10.3 1.0 N2 A:PZO404 3.1 12.2 1.0 CE1 A:HIS67 3.1 13.1 1.0 C5 A:PZO404 3.2 12.8 1.0 CB A:CYS46 3.3 11.3 1.0 CB A:CYS174 3.4 12.3 1.0 C4N A:NAJ403 3.5 10.5 1.0 C6N A:NAJ403 3.9 11.5 1.0 OG A:SER48 4.1 11.6 1.0 CB A:SER48 4.2 12.0 1.0 CG A:HIS67 4.2 12.3 1.0 ND1 A:HIS67 4.2 12.3 1.0 C3 A:PZO404 4.3 14.0 1.0 C4 A:PZO404 4.3 13.8 1.0 NH2 A:ARG369 4.5 14.5 1.0 CE2 A:PHE93 4.6 13.0 1.0 CA A:CYS174 4.7 10.9 1.0 CA A:CYS46 4.7 12.5 1.0 OE2 A:GLU68 4.8 14.7 1.0 CZ A:PHE93 4.9 13.2 1.0 C3N A:NAJ403 5.0 11.5 1.0 N A:SER48 5.0 14.1 1.0

Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:14.6 occ:1.00 SG A:CYS100 2.3 15.2 1.0 SG A:CYS103 2.3 14.4 1.0 SG A:CYS111 2.3 13.8 1.0 SG A:CYS97 2.4 15.9 1.0 CB A:CYS111 3.3 15.4 1.0 CB A:CYS103 3.4 15.7 1.0 CB A:CYS100 3.4 15.7 1.0 CB A:CYS97 3.4 16.0 1.0 N A:CYS97 3.6 14.3 1.0 CA A:CYS111 3.7 13.7 1.0 N A:CYS100 3.9 18.4 1.0 CA A:CYS97 3.9 16.6 1.0 N A:GLY98 4.0 17.1 1.0 N A:LEU112 4.0 14.1 1.0 CA A:CYS100 4.2 17.1 1.0 N A:CYS103 4.2 13.8 1.0 C A:CYS111 4.3 14.3 1.0 CA A:CYS103 4.3 14.6 1.0 C A:CYS97 4.4 17.2 1.0 N A:LYS99 4.5 20.9 1.0 C A:GLN96 4.6 14.6 1.0 C A:CYS100 4.8 16.0 1.0 N A:LYS113 4.9 13.8 1.0 CG A:LYS113 4.9 20.1 1.0 O A:CYS100 4.9 16.8 1.0 CA A:GLN96 4.9 13.9 1.0 O A:HOH820 4.9 33.4 1.0 CA A:GLY98 5.0 17.9 1.0

Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:17.0 occ:1.00 NE2 B:HIS67 2.1 16.7 1.0 N2 B:PZO404 2.1 14.4 1.0 SG B:CYS174 2.3 19.1 1.0 SG B:CYS46 2.3 16.7 1.0 C3 B:PZO404 3.0 16.4 1.0 CE1 B:HIS67 3.0 16.7 1.0 CD2 B:HIS67 3.1 15.4 1.0 C5N B:NAJ403 3.2 14.8 1.0 N1 B:PZO404 3.2 16.5 1.0 CB B:CYS174 3.3 15.1 1.0 CB B:CYS46 3.3 14.6 1.0 C4N B:NAJ403 3.6 15.9 1.0 C6N B:NAJ403 3.9 15.2 1.0 OG B:SER48 4.1 15.3 1.0 CB B:SER48 4.1 15.2 1.0 ND1 B:HIS67 4.2 14.8 1.0 CG B:HIS67 4.2 14.7 1.0 C4 B:PZO404 4.2 16.5 1.0 C5 B:PZO404 4.3 17.3 1.0 NH2 B:ARG369 4.5 19.4 1.0 CE2 B:PHE93 4.6 15.2 1.0 CA B:CYS174 4.6 14.3 1.0 CA B:CYS46 4.8 17.5 1.0 OE2 B:GLU68 4.8 17.4 1.0 CZ B:PHE93 4.9 17.0 1.0 N B:SER48 5.0 16.1 1.0 C3N B:NAJ403 5.0 13.5 1.0

Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:17.5 occ:1.00 SG B:CYS100 2.3 17.5 1.0 SG B:CYS111 2.3 17.2 1.0 SG B:CYS97 2.3 19.0 1.0 SG B:CYS103 2.4 17.1 1.0 CB B:CYS97 3.4 16.2 1.0 CB B:CYS100 3.4 19.0 1.0 CB B:CYS111 3.4 15.7 1.0 CB B:CYS103 3.4 17.2 1.0 N B:CYS97 3.6 17.0 1.0 CA B:CYS111 3.7 16.6 1.0 N B:CYS100 3.9 20.8 1.0 CA B:CYS97 3.9 18.2 1.0 N B:GLY98 4.0 20.1 1.0 N B:LEU112 4.0 17.4 1.0 CA B:CYS100 4.2 20.4 1.0 N B:CYS103 4.2 16.2 1.0 C B:CYS111 4.3 16.6 1.0 C B:CYS97 4.3 20.9 1.0 CA B:CYS103 4.4 17.3 1.0 N B:LYS99 4.4 21.6 1.0 C B:GLN96 4.6 16.2 1.0 N B:LYS113 4.8 17.6 1.0 C B:CYS100 4.9 18.5 1.0 CG B:LYS113 4.9 22.8 1.0 O B:HOH786 4.9 33.5 1.0 CA B:GLN96 5.0 16.1 1.0 O B:CYS100 5.0 17.4 1.0 CA B:GLY98 5.0 20.6 1.0

B.V.Plapp, E.G.Kovaleva. Histidine-51 Facilitates Deprotonation of the Zinc-Bound Ligand During Catalysis By Horse Liver Alcohol Dehydrogenase To Be Published.