Zinc in PDB 1qlj: Horse Liver Alcohol Dehydrogenase Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogenase Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr, PDB code: 1qlj was solved by S.Ramaswamy, B.V.Plapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.140, 72.920, 180.250, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 25.7

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr (pdb code 1qlj). 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 Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr, PDB code: 1qlj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Horse Liver Alcohol Dehydrogenase Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr


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 Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn375 b:32.2 occ:1.00 O A:HOH2087 2.0 28.1 1.0 NE2 A:HIS67 2.0 22.3 1.0 SG A:CYS174 2.3 20.6 1.0 SG A:CYS46 2.3 31.9 1.0 CE1 A:HIS67 2.9 18.4 1.0 CD2 A:HIS67 3.1 19.0 1.0 CB A:CYS46 3.3 27.6 1.0 CB A:CYS174 3.6 14.4 1.0 ND1 A:HIS67 4.1 17.4 1.0 CG A:HIS67 4.2 18.1 1.0 CB A:SER48 4.2 23.9 1.0 OG A:SER48 4.3 22.7 1.0 CA A:CYS46 4.7 26.0 1.0 CE2 A:PHE93 4.8 12.1 1.0 CA A:CYS174 4.9 14.2 1.0 NH2 A:ARG369 4.9 33.4 1.0 N A:SER48 5.0 27.6 1.0

Zinc binding site 2 out of 2 in the Horse Liver Alcohol Dehydrogenase Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr


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 Apo Enzyme Double Mutant of Gly 293 Ala and Pro 295 Thr within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn376 b:23.2 occ:1.00 SG A:CYS100 2.3 27.6 1.0 SG A:CYS97 2.3 21.8 1.0 SG A:CYS103 2.3 12.5 1.0 SG A:CYS111 2.3 23.5 1.0 CB A:CYS103 3.2 18.9 1.0 CB A:CYS111 3.4 21.3 1.0 CB A:CYS97 3.5 20.6 1.0 CB A:CYS100 3.5 29.0 1.0 N A:CYS97 3.5 19.2 1.0 N A:CYS100 3.7 29.4 1.0 N A:GLY98 3.8 23.7 1.0 CA A:CYS97 3.9 21.1 1.0 CA A:CYS111 3.9 20.9 1.0 N A:CYS103 4.1 21.1 1.0 N A:LYS99 4.1 27.7 1.0 CA A:CYS100 4.1 28.8 1.0 N A:LEU112 4.2 19.0 1.0 C A:CYS97 4.2 22.2 1.0 CA A:CYS103 4.2 20.0 1.0 C A:CYS111 4.5 20.8 1.0 C A:GLN96 4.5 19.7 1.0 O A:CYS100 4.6 27.5 1.0 CA A:GLY98 4.7 25.5 1.0 C A:CYS100 4.7 29.4 1.0 C A:LYS99 4.7 30.1 1.0 CG A:LYS113 4.8 21.2 1.0 N A:LYS113 4.8 18.5 1.0 CA A:GLN96 4.9 20.1 1.0 C A:GLY98 4.9 27.0 1.0 CA A:LYS99 4.9 29.4 1.0 O A:HOH2027 5.0 16.1 1.0

S.Ramaswamy, D.H.Park, B.V.Plapp. Substitutions in the Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer Biochemistry V. 38 13951 1999.
ISSN: ISSN 0006-2960
PubMed: 10529241
DOI: 10.1021/BI991731I