Zinc in PDB 5vjg: Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine, PDB code: 5vjg was solved by B.V.Plapp, S.Baskar Raj, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	55.450, 73.700, 181.140, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 28.4

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine (pdb code 5vjg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine, PDB code: 5vjg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine


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 Dehydrogenase Complexed with 2,2'Bipyridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:40.4 occ:1.00 SG A:CYS174 2.2 36.4 1.0 NE2 A:HIS67 2.3 34.7 1.0 SG A:CYS46 2.4 38.3 1.0 N1 A:0BP403 2.5 47.0 1.0 N8 A:0BP403 2.6 48.6 1.0 CD2 A:HIS67 3.2 35.5 1.0 CE1 A:HIS67 3.3 32.5 1.0 C6 A:0BP403 3.4 51.4 1.0 CB A:CYS174 3.4 40.9 1.0 C2 A:0BP403 3.4 54.2 1.0 C9 A:0BP403 3.5 47.1 1.0 C7 A:0BP403 3.5 52.9 1.0 CB A:CYS46 3.6 35.2 1.0 CB A:SER48 4.1 29.5 1.0 OG A:SER48 4.2 29.9 1.0 ND1 A:HIS67 4.4 31.0 1.0 CG A:HIS67 4.4 29.3 1.0 C5 A:0BP403 4.7 45.6 1.0 CA A:CYS174 4.7 33.1 1.0 C3 A:0BP403 4.8 48.1 1.0 CE2 A:PHE93 4.8 30.5 1.0 C10 A:0BP403 4.8 48.5 1.0 CZ A:PHE93 4.8 29.1 1.0 C12 A:0BP403 4.8 50.2 1.0 N A:SER48 4.8 33.7 1.0

Zinc binding site 2 out of 2 in the Horse Liver Alcohol Dehydrogenase Complexed with 2,2'Bipyridine


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 Dehydrogenase Complexed with 2,2'Bipyridine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:39.5 occ:1.00 SG A:CYS103 2.0 34.0 1.0 SG A:CYS97 2.4 39.6 1.0 SG A:CYS100 2.4 43.0 1.0 SG A:CYS111 2.4 38.2 1.0 CB A:CYS111 3.3 38.5 1.0 CB A:CYS103 3.4 41.7 1.0 CB A:CYS100 3.4 44.5 1.0 CB A:CYS97 3.5 35.1 1.0 N A:CYS97 3.6 36.8 1.0 CA A:CYS111 3.7 34.0 1.0 N A:CYS100 3.8 46.6 1.0 CA A:CYS97 3.9 37.3 1.0 N A:GLY98 4.0 44.4 1.0 N A:LEU112 4.0 32.9 1.0 N A:CYS103 4.1 39.5 1.0 CA A:CYS100 4.2 46.0 1.0 C A:CYS111 4.3 35.7 1.0 C A:CYS97 4.3 44.4 1.0 CA A:CYS103 4.3 34.9 1.0 N A:LYS99 4.5 39.7 1.0 C A:GLN96 4.5 34.1 1.0 CG A:LYS113 4.7 41.1 1.0 N A:LYS113 4.7 32.5 1.0 C A:CYS100 4.8 41.2 1.0 CA A:GLN96 4.8 40.0 1.0 O A:CYS100 4.9 37.5 1.0 CA A:GLY98 5.0 44.5 1.0 C A:LYS99 5.0 54.7 1.0

B.V.Plapp, B.R.Savarimuthu, D.J.Ferraro, J.K.Rubach, E.N.Brown, S.Ramaswamy. Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis. Biochemistry V. 56 3632 2017.
ISSN: ISSN 1520-4995
PubMed: 28640600
DOI: 10.1021/ACS.BIOCHEM.7B00446