Zinc in PDB 1e3i: Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor

All present enzymatic activity of Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor:
1.1.1.1;

The structure of Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor, PDB code: 1e3i was solved by S.Svensson, J.O.Hoog, G.Schneider, T.Sandalova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.08
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.253, 81.070, 102.187, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 22.8

The binding sites of Zinc atom in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor (pdb code 1e3i). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor, PDB code: 1e3i:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn380 b:22.3 occ:1.00 O9 A:CXF378 2.2 24.5 1.0 NE2 A:HIS67 2.2 22.3 1.0 SG A:CYS178 2.3 16.2 1.0 SG A:CYS46 2.3 21.6 1.0 C7 A:CXF378 2.7 25.2 1.0 CB A:CYS46 3.1 22.1 1.0 CE1 A:HIS67 3.1 20.5 1.0 CD2 A:HIS67 3.2 20.5 1.0 CB A:CYS178 3.5 14.2 1.0 N8 A:CXF378 4.0 28.2 1.0 O A:HOH2180 4.0 18.3 1.0 C5N A:NAI377 4.1 21.4 1.0 OG1 A:THR48 4.1 22.5 1.0 CB A:THR48 4.2 23.8 1.0 ND1 A:HIS67 4.2 18.5 1.0 C6N A:NAI377 4.3 21.1 1.0 CG A:HIS67 4.3 20.5 1.0 CA A:CYS46 4.6 23.9 1.0 OE1 A:GLU68 4.8 21.3 1.0 CA A:CYS178 4.8 16.3 1.0 NH2 A:ARG371 4.9 19.9 1.0 CE2 A:PHE93 4.9 18.2 1.0 C A:CYS178 5.0 16.2 1.0 N A:GLY179 5.0 18.0 1.0 C4N A:NAI377 5.0 18.3 1.0

Zinc binding site 2 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn381 b:26.4 occ:1.00 SG A:CYS103 2.3 24.8 1.0 SG A:CYS111 2.3 25.2 1.0 SG A:CYS100 2.3 25.2 1.0 SG A:CYS97 2.3 23.7 1.0 CB A:CYS103 3.3 23.8 1.0 CB A:CYS111 3.4 23.1 1.0 CB A:CYS100 3.5 23.4 1.0 N A:CYS97 3.5 22.1 1.0 CB A:CYS97 3.5 20.7 1.0 N A:GLY112 3.7 24.0 1.0 CA A:CYS111 3.7 22.0 1.0 N A:LYS98 3.8 22.8 1.0 CA A:CYS97 3.9 22.5 1.0 O A:HOH2064 4.0 37.1 1.0 N A:CYS100 4.1 24.7 1.0 C A:CYS111 4.2 23.1 1.0 C A:CYS97 4.2 22.9 1.0 N A:CYS103 4.2 21.5 1.0 N A:ARG99 4.2 24.2 1.0 CA A:CYS103 4.3 22.4 1.0 CA A:CYS100 4.4 24.9 1.0 C A:GLN96 4.5 22.0 1.0 C A:ARG99 4.6 25.3 1.0 CA A:LYS98 4.7 22.3 1.0 N A:LYS113 4.7 31.1 1.0 CA A:GLY112 4.7 27.5 1.0 CA A:GLN96 4.8 20.9 1.0 C A:LYS98 4.9 23.1 1.0 O A:CYS100 4.9 25.7 1.0 C A:CYS100 4.9 25.0 1.0

Zinc binding site 3 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn380 b:20.4 occ:1.00 C7 B:CXF378 2.1 25.3 1.0 NE2 B:HIS67 2.2 22.1 1.0 O9 B:CXF378 2.2 24.6 1.0 SG B:CYS46 2.3 19.4 1.0 SG B:CYS178 2.3 20.0 1.0 CE1 B:HIS67 3.0 23.1 1.0 CB B:CYS46 3.3 20.9 1.0 CD2 B:HIS67 3.3 20.6 1.0 N8 B:CXF378 3.4 28.3 1.0 CB B:CYS178 3.6 19.7 1.0 O B:HOH2177 4.0 20.6 1.0 OG1 B:THR48 4.1 21.9 1.0 C5N B:NAI377 4.2 16.6 1.0 CB B:THR48 4.2 23.7 1.0 ND1 B:HIS67 4.2 24.2 1.0 C6N B:NAI377 4.4 19.4 1.0 CG B:HIS67 4.4 21.5 1.0 C1 B:CXF378 4.6 27.3 1.0 CE2 B:PHE93 4.7 18.1 1.0 CA B:CYS46 4.8 20.9 1.0 NH2 B:ARG371 4.8 15.5 1.0 OE1 B:GLU68 4.8 14.2 1.0 CA B:CYS178 4.9 20.2 1.0 N B:GLY179 5.0 18.4 1.0

Zinc binding site 4 out of 4 in the Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Mouse Class II Alcohol Dehydrogenase Complex with Nadh and Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn381 b:27.8 occ:1.00 SG B:CYS100 2.3 36.4 1.0 SG B:CYS111 2.3 25.2 1.0 SG B:CYS103 2.3 26.6 1.0 SG B:CYS97 2.3 20.6 1.0 N B:CYS97 3.4 28.5 1.0 CB B:CYS111 3.5 25.5 1.0 CB B:CYS103 3.5 34.5 1.0 CB B:CYS97 3.6 28.4 1.0 CB B:CYS100 3.6 44.8 1.0 N B:GLY112 3.7 27.5 1.0 N B:LYS98 3.7 38.5 1.0 CA B:CYS111 3.8 27.2 1.0 CA B:CYS97 3.9 31.1 1.0 N B:CYS100 4.0 47.7 1.0 C B:CYS111 4.1 27.9 1.0 C B:CYS97 4.2 34.9 1.0 N B:CYS103 4.3 36.2 1.0 C B:GLN96 4.3 27.4 1.0 N B:ARG99 4.3 46.8 1.0 CA B:CYS100 4.4 45.8 1.0 CA B:CYS103 4.4 36.5 1.0 CA B:GLN96 4.5 25.7 1.0 N B:LYS113 4.6 29.7 1.0 CA B:GLY112 4.6 27.9 1.0 CA B:LYS98 4.6 42.0 1.0 C B:CYS100 4.9 47.1 1.0 C B:ARG99 4.9 47.8 1.0

S.Svensson, J.O.Hoeoeg, G.Schneider, T.Sandalova. Crystal Structure of Mouse Class II Alcohol Dehydrogenase Reveal Determinants of Substrate Specificity and Catalytic Efficiency J.Mol.Biol. V. 302 441 2000.
ISSN: ISSN 0022-2836
PubMed: 10970744
DOI: 10.1006/JMBI.2000.4039