Zinc in PDB 1mgo: Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant, PDB code: 1mgo was solved by J.K.Rubach, B.V.Plapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.20
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	44.144, 51.308, 93.481, 91.98, 103.01, 109.81
R / Rfree (%)	18.8 / 20.9

The structure of Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant also contains other interesting chemical elements:

Fluorine

(F)

10 atoms

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant (pdb code 1mgo). 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 Dehydrogenase PHE93ALA Mutant, PDB code: 1mgo:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant


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 PHE93ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn375 b:19.7 occ:1.00 NE2 A:HIS67 2.0 15.7 1.0 O A:HOH570 2.1 19.5 1.0 SG A:CYS174 2.2 17.8 1.0 SG A:CYS46 2.3 18.2 1.0 CE1 A:HIS67 3.0 17.2 1.0 CD2 A:HIS67 3.1 15.5 1.0 CB A:CYS174 3.3 16.2 1.0 CB A:CYS46 3.3 17.9 1.0 C5N A:NAD377 3.5 17.8 1.0 ND1 A:HIS67 4.1 16.3 1.0 C4N A:NAD377 4.1 18.3 1.0 CG A:HIS67 4.2 15.4 1.0 C6N A:NAD377 4.2 15.7 1.0 CB A:SER48 4.2 17.1 1.0 OG A:SER48 4.3 18.3 1.0 NH2 A:ARG369 4.6 19.7 1.0 OE2 A:GLU68 4.6 19.8 1.0 CA A:CYS174 4.6 15.7 1.0 CA A:CYS46 4.8 17.9 1.0 O A:HOH571 4.8 21.3 1.0 N A:GLY175 4.9 14.8 1.0 C A:CYS174 5.0 15.2 1.0

Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant


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 PHE93ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn376 b:18.1 occ:1.00 SG A:CYS97 2.3 21.4 1.0 SG A:CYS103 2.3 17.4 1.0 SG A:CYS100 2.3 18.2 1.0 SG A:CYS111 2.4 17.5 1.0 CB A:CYS103 3.4 15.8 1.0 CB A:CYS100 3.4 17.5 1.0 CB A:CYS111 3.4 16.2 1.0 CB A:CYS97 3.4 16.9 1.0 N A:CYS97 3.5 16.3 1.0 CA A:CYS111 3.8 15.2 1.0 N A:CYS100 3.8 19.6 1.0 CA A:CYS97 3.9 17.4 1.0 N A:GLY98 4.0 18.7 1.0 N A:LEU112 4.1 17.4 1.0 CA A:CYS100 4.2 19.5 1.0 N A:CYS103 4.2 16.2 1.0 C A:CYS97 4.3 18.9 1.0 C A:CYS111 4.3 16.4 1.0 CA A:CYS103 4.4 16.5 1.0 N A:LYS99 4.5 21.6 1.0 C A:GLN96 4.7 16.3 1.0 C A:CYS100 4.8 18.6 1.0 N A:LYS113 4.9 17.3 1.0 O A:CYS100 4.9 17.6 1.0 CG A:LYS113 4.9 21.5 1.0 CA A:GLN96 5.0 15.5 1.0 CA A:GLY98 5.0 19.7 1.0 C A:LYS99 5.0 22.3 1.0

Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant


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 Dehydrogenase PHE93ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn375 b:16.8 occ:1.00 NE2 B:HIS67 2.0 14.0 1.0 O B:HOH838 2.1 19.0 1.0 SG B:CYS174 2.3 15.6 1.0 SG B:CYS46 2.3 15.4 1.0 CE1 B:HIS67 3.0 13.9 1.0 CD2 B:HIS67 3.1 14.8 1.0 CB B:CYS174 3.3 14.0 1.0 CB B:CYS46 3.4 14.4 1.0 C5N B:NAD377 3.5 16.7 1.0 O2 B:MPD602 4.0 29.9 1.0 C6N B:NAD377 4.1 14.1 1.0 C4N B:NAD377 4.1 15.4 1.0 ND1 B:HIS67 4.1 15.0 1.0 OG B:SER48 4.1 15.3 1.0 CB B:SER48 4.2 14.8 1.0 CG B:HIS67 4.2 14.2 1.0 OE2 B:GLU68 4.6 17.1 1.0 NH2 B:ARG369 4.6 18.4 1.0 CA B:CYS174 4.6 13.6 1.0 CA B:CYS46 4.8 15.3 1.0 N B:SER48 4.9 15.3 1.0 O B:HOH626 4.9 19.2 1.0 C B:CYS174 5.0 14.2 1.0 N B:GLY175 5.0 13.9 1.0

Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase PHE93ALA Mutant


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 Dehydrogenase PHE93ALA Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn376 b:15.3 occ:1.00 SG B:CYS103 2.3 14.5 1.0 SG B:CYS97 2.3 17.1 1.0 SG B:CYS100 2.4 15.7 1.0 SG B:CYS111 2.4 14.8 1.0 CB B:CYS111 3.3 13.7 1.0 CB B:CYS103 3.3 15.9 1.0 CB B:CYS100 3.4 16.9 1.0 CB B:CYS97 3.4 13.7 1.0 N B:CYS97 3.6 12.8 1.0 CA B:CYS111 3.7 13.4 1.0 N B:CYS100 3.8 17.6 1.0 CA B:CYS97 4.0 14.7 1.0 N B:GLY98 4.0 16.9 1.0 N B:LEU112 4.0 13.9 1.0 CA B:CYS100 4.2 18.0 1.0 N B:CYS103 4.2 15.2 1.0 CA B:CYS103 4.3 15.1 1.0 C B:CYS111 4.4 14.2 1.0 C B:CYS97 4.4 15.6 1.0 N B:LYS99 4.5 18.2 1.0 C B:GLN96 4.6 13.9 1.0 C B:CYS100 4.8 16.9 1.0 N B:LYS113 4.9 15.4 1.0 CG B:LYS113 4.9 17.5 1.0 O B:CYS100 4.9 16.3 1.0 CA B:GLN96 4.9 12.8 1.0 CA B:GLY98 5.0 17.5 1.0 C B:LYS99 5.0 20.2 1.0

J.K.Rubach, B.V.Plapp. Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases As Determined By uc(Nmr) and X-Ray Crystallographic Studies Biochemistry V. 41 15770 2002.
ISSN: ISSN 0006-2960
PubMed: 12501206
DOI: 10.1021/BI026581H