Zinc in PDB 8g39: Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide

All present enzymatic activity of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide, PDB code: 8g39 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)	19.91 / 1.42
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	44.08, 50.92, 92.74, 92.1, 102.95, 109.68
R / Rfree (%)	14.6 / 19.1

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide (pdb code 8g39). 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 Nadh and N-Cyclohexylformamide, PDB code: 8g39:
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 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 Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:17.6 occ:1.00 NE2 A:HIS67 2.1 15.8 1.0 O9 A:CXF404 2.1 17.8 1.0 SG A:CYS174 2.3 16.7 1.0 SG A:CYS46 2.3 17.1 1.0 C7 A:CXF404 2.9 24.9 1.0 CD2 A:HIS67 3.0 15.7 1.0 CB A:CYS46 3.2 16.6 1.0 CE1 A:HIS67 3.2 17.5 1.0 CB A:CYS174 3.3 13.1 1.0 C5N A:NAI403 3.4 14.5 1.0 C6N A:NAI403 4.0 14.0 1.0 C4N A:NAI403 4.0 14.0 1.0 OG A:SER48 4.1 16.4 1.0 CG A:HIS67 4.2 14.8 1.0 N8 A:CXF404 4.2 27.2 1.0 CB A:SER48 4.2 16.0 1.0 ND1 A:HIS67 4.2 15.2 1.0 NH2 A:ARG369 4.4 18.9 1.0 OE2 A:GLU68 4.6 18.6 1.0 CA A:CYS46 4.6 17.5 1.0 CA A:CYS174 4.6 12.4 1.0 CE2 A:PHE93 4.9 15.2 1.0 N A:GLY175 4.9 14.2 1.0 N A:SER48 4.9 15.7 1.0 C A:CYS174 5.0 13.2 1.0

Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed 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 Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:16.8 occ:1.00 SG A:CYS100 2.3 17.0 1.0 SG A:CYS111 2.3 16.7 1.0 SG A:CYS103 2.3 16.3 1.0 SG A:CYS97 2.3 18.0 1.0 CB A:CYS111 3.2 16.2 1.0 CB A:CYS103 3.4 17.0 1.0 CB A:CYS100 3.4 17.1 1.0 CB A:CYS97 3.5 16.6 1.0 N A:CYS97 3.6 14.6 1.0 CA A:CYS111 3.7 16.1 1.0 N A:CYS100 3.9 20.4 1.0 CA A:CYS97 4.0 16.2 1.0 N A:GLY98 4.0 18.5 1.0 N A:LEU112 4.0 17.2 1.0 N A:CYS103 4.2 15.7 1.0 CA A:CYS100 4.2 15.6 1.0 C A:CYS111 4.3 14.9 1.0 CA A:CYS103 4.3 16.3 1.0 C A:CYS97 4.4 18.1 1.0 N A:LYS99 4.5 20.8 1.0 C A:GLN96 4.7 16.6 1.0 N A:LYS113 4.8 15.2 1.0 C A:CYS100 4.9 15.9 1.0 CA A:GLN96 5.0 15.5 1.0 O A:CYS100 5.0 17.9 1.0 O A:HOH804 5.0 31.9 1.0 CG A:LYS113 5.0 22.2 1.0 N A:CYS111 5.0 14.8 1.0 CA A:GLY98 5.0 18.5 1.0

Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed 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 3 of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:20.6 occ:1.00 O9 B:CXF404 2.0 22.3 1.0 NE2 B:HIS67 2.1 21.1 1.0 SG B:CYS174 2.2 21.0 1.0 SG B:CYS46 2.3 20.2 1.0 C7 B:CXF404 2.8 26.7 1.0 CD2 B:HIS67 3.0 18.3 1.0 CE1 B:HIS67 3.1 22.3 1.0 CB B:CYS46 3.2 18.6 1.0 CB B:CYS174 3.2 17.4 1.0 C5N B:NAI403 3.4 17.6 1.0 C6N B:NAI403 4.0 17.7 1.0 C4N B:NAI403 4.0 18.5 1.0 N8 B:CXF404 4.1 25.1 1.0 OG B:SER48 4.1 19.4 1.0 ND1 B:HIS67 4.2 19.8 1.0 CG B:HIS67 4.2 20.4 1.0 CB B:SER48 4.2 17.3 1.0 NH2 B:ARG369 4.3 22.1 1.0 OE2 B:GLU68 4.5 21.0 1.0 CA B:CYS174 4.6 17.6 1.0 CA B:CYS46 4.7 21.3 1.0 N B:GLY175 4.8 19.9 1.0 C B:CYS174 4.9 17.5 1.0 CE2 B:PHE93 4.9 18.5 1.0 N B:SER48 4.9 19.2 1.0

Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed 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 4 of Horse Liver Alcohol Dehydrogense His-51-Gln Form Complexed with Nadh and N-Cyclohexylformamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:19.2 occ:1.00 SG B:CYS111 2.3 19.2 1.0 SG B:CYS100 2.3 19.9 1.0 SG B:CYS97 2.4 20.7 1.0 SG B:CYS103 2.4 19.1 1.0 CB B:CYS111 3.3 19.1 1.0 CB B:CYS103 3.4 18.9 1.0 CB B:CYS100 3.4 21.1 1.0 CB B:CYS97 3.4 17.5 1.0 N B:CYS97 3.6 18.9 1.0 CA B:CYS111 3.7 18.0 1.0 N B:CYS100 3.9 21.7 1.0 CA B:CYS97 3.9 18.2 1.0 N B:GLY98 3.9 23.0 1.0 N B:LEU112 3.9 19.5 1.0 N B:CYS103 4.2 18.8 1.0 CA B:CYS100 4.2 20.2 1.0 C B:CYS111 4.2 16.8 1.0 C B:CYS97 4.3 20.9 1.0 CA B:CYS103 4.4 18.7 1.0 N B:LYS99 4.5 22.8 1.0 C B:GLN96 4.6 17.3 1.0 N B:LYS113 4.8 19.4 1.0 C B:CYS100 4.9 18.9 1.0 CA B:GLN96 4.9 16.8 1.0 CG B:LYS113 5.0 24.1 1.0 O B:CYS100 5.0 19.3 1.0 O B:HOH754 5.0 31.9 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.