Zinc in PDB 5vkr: Horse Liver Alcohol Dehydrogenase Complexed with Adenosine-5- Diphosphoribose

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase Complexed with Adenosine-5- Diphosphoribose:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogenase Complexed with Adenosine-5- Diphosphoribose, PDB code: 5vkr was solved by B.V.Plapp, J.K.Rubach, S.Ramaswamy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	55.370, 74.270, 180.950, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 24.8

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase Complexed with Adenosine-5- Diphosphoribose (pdb code 5vkr). 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 Adenosine-5- Diphosphoribose, PDB code: 5vkr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Horse Liver Alcohol Dehydrogenase Complexed with Adenosine-5- Diphosphoribose


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 Adenosine-5- Diphosphoribose within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:54.9 occ:1.00 NE2 A:HIS67 2.1 49.5 1.0 SG A:CYS174 2.3 53.8 1.0 O A:HOH502 2.3 54.3 1.0 SG A:CYS46 2.4 62.0 1.0 CE1 A:HIS67 2.9 49.6 1.0 CD2 A:HIS67 3.2 49.1 1.0 CB A:CYS174 3.3 55.3 1.0 CB A:CYS46 3.3 53.0 1.0 OE2 A:GLU68 4.0 95.9 1.0 ND1 A:HIS67 4.1 47.1 1.0 OG A:SER48 4.1 46.3 1.0 CG A:HIS67 4.3 45.5 1.0 CB A:SER48 4.3 51.1 1.0 NH2 A:ARG369 4.4 94.9 1.0 CA A:CYS174 4.7 47.5 1.0 CA A:CYS46 4.8 48.4 1.0

Zinc binding site 2 out of 2 in the Horse Liver Alcohol Dehydrogenase Complexed with Adenosine-5- Diphosphoribose


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 Adenosine-5- Diphosphoribose within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:44.3 occ:1.00 SG A:CYS103 2.3 41.1 1.0 SG A:CYS100 2.3 44.0 1.0 SG A:CYS97 2.4 48.7 1.0 SG A:CYS111 2.4 43.1 1.0 CB A:CYS111 3.3 44.0 1.0 CB A:CYS97 3.5 43.2 1.0 CB A:CYS103 3.5 41.6 1.0 CB A:CYS100 3.5 52.2 1.0 N A:CYS97 3.6 40.6 1.0 CA A:CYS111 3.7 38.7 1.0 N A:LEU112 3.9 43.6 1.0 N A:CYS100 4.0 48.9 1.0 CA A:CYS97 4.0 47.1 1.0 N A:GLY98 4.1 56.4 1.0 N A:CYS103 4.2 40.6 1.0 C A:CYS111 4.2 42.7 1.0 CA A:CYS100 4.3 48.9 1.0 CA A:CYS103 4.4 41.6 1.0 C A:CYS97 4.5 57.0 1.0 N A:LYS99 4.6 56.4 1.0 CG A:LYS113 4.7 51.5 1.0 C A:GLN96 4.7 38.8 1.0 N A:LYS113 4.8 40.2 1.0 C A:CYS100 4.9 43.8 1.0 CA A:GLN96 5.0 38.4 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