Zinc in PDB 1n8k: Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole

All present enzymatic activity of Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole:
1.1.1.1;

The structure of Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole, PDB code: 1n8k 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 / 1.13
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	44.310, 51.380, 92.670, 91.94, 102.97, 109.93
R / Rfree (%)	14.4 / 16.7

The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole (pdb code 1n8k). 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 VAL292THR Mutant Complexed to Nad+ and Pyrazole, PDB code: 1n8k:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole


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 VAL292THR Mutant Complexed to Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn375 b:12.1 occ:1.00 NE2 A:HIS67 2.0 12.5 1.0 N1 A:PZO378 2.1 13.5 1.0 SG A:CYS174 2.3 12.8 1.0 SG A:CYS46 2.3 11.5 1.0 CE1 A:HIS67 3.0 11.6 1.0 CD2 A:HIS67 3.0 11.2 1.0 C5 A:PZO378 3.1 14.3 1.0 N2 A:PZO378 3.2 15.5 1.0 C5N A:NAJ377 3.2 11.1 1.0 CB A:CYS46 3.3 12.9 1.0 CB A:CYS174 3.4 11.2 1.0 C4N A:NAJ377 3.6 12.7 1.0 C6N A:NAJ377 4.0 10.6 1.0 OG A:SER48 4.1 13.9 1.0 ND1 A:HIS67 4.1 10.6 1.0 CB A:SER48 4.1 11.6 1.0 CG A:HIS67 4.2 10.2 1.0 C4 A:PZO378 4.3 14.4 1.0 C3 A:PZO378 4.3 14.9 1.0 NH2 A:ARG369 4.6 15.7 1.0 CE2 A:PHE93 4.7 12.7 1.0 CA A:CYS174 4.7 10.4 1.0 CA A:CYS46 4.8 12.7 1.0 OE2 A:GLU68 4.9 16.6 1.0 CZ A:PHE93 4.9 12.9 1.0 N A:SER48 5.0 11.1 1.0

Zinc binding site 2 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole


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 VAL292THR Mutant Complexed to Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn376 b:13.1 occ:1.00 SG A:CYS111 2.3 12.5 1.0 SG A:CYS100 2.3 13.0 1.0 SG A:CYS97 2.3 14.8 1.0 SG A:CYS103 2.4 12.6 1.0 CB A:CYS111 3.3 12.2 1.0 CB A:CYS103 3.4 13.4 1.0 CB A:CYS97 3.4 16.5 1.0 CB A:CYS100 3.4 14.8 1.0 N A:CYS97 3.5 12.7 1.0 CA A:CYS111 3.7 11.8 1.0 N A:CYS100 3.9 16.6 1.0 CA A:CYS97 3.9 14.9 1.0 N A:LEU112 4.0 13.2 1.0 N A:GLY98 4.0 14.4 1.0 N A:CYS103 4.2 13.1 1.0 CA A:CYS100 4.2 14.6 1.0 C A:CYS111 4.3 12.1 1.0 C A:CYS97 4.4 15.3 1.0 CA A:CYS103 4.4 12.5 1.0 N A:LYS99 4.5 17.1 1.0 C A:GLN96 4.6 12.6 1.0 N A:LYS113 4.8 13.2 1.0 C A:CYS100 4.9 14.3 1.0 CG A:LYS113 4.9 16.8 1.0 O A:CYS100 4.9 14.9 1.0 CA A:GLN96 5.0 12.2 1.0 O A:HOH1192 5.0 33.4 1.0 CA A:GLY98 5.0 16.4 1.0

Zinc binding site 3 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole


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 VAL292THR Mutant Complexed to Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn375 b:15.2 occ:1.00 NE2 B:HIS67 2.0 14.5 1.0 N1 B:PZO378 2.1 14.5 1.0 SG B:CYS174 2.3 15.7 1.0 SG B:CYS46 2.3 14.9 1.0 CE1 B:HIS67 3.0 13.2 1.0 CD2 B:HIS67 3.0 14.7 1.0 C5 B:PZO378 3.1 16.3 1.0 N2 B:PZO378 3.2 17.2 1.0 C5N B:NAJ377 3.2 14.5 1.0 CB B:CYS46 3.3 15.5 1.0 CB B:CYS174 3.4 14.1 1.0 C4N B:NAJ377 3.6 15.1 1.0 C6N B:NAJ377 4.0 14.2 1.0 OG B:SER48 4.1 15.9 1.0 ND1 B:HIS67 4.1 14.0 1.0 CB B:SER48 4.2 14.8 1.0 CG B:HIS67 4.2 13.0 1.0 C4 B:PZO378 4.3 17.4 1.0 C3 B:PZO378 4.3 17.6 1.0 NH2 B:ARG369 4.5 16.9 1.0 CE2 B:PHE93 4.7 15.2 1.0 CA B:CYS174 4.7 13.9 1.0 CA B:CYS46 4.8 15.3 1.0 OE2 B:GLU68 4.9 19.8 1.0 CZ B:PHE93 4.9 16.8 1.0 N B:SER48 5.0 14.6 1.0

Zinc binding site 4 out of 4 in the Horse Liver Alcohol Dehydrogenase VAL292THR Mutant Complexed to Nad+ and Pyrazole


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 VAL292THR Mutant Complexed to Nad+ and Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn376 b:15.8 occ:1.00 SG B:CYS111 2.3 15.2 1.0 SG B:CYS100 2.3 15.9 1.0 SG B:CYS97 2.4 18.2 1.0 SG B:CYS103 2.4 14.7 1.0 CB B:CYS111 3.3 14.0 1.0 CB B:CYS103 3.4 15.8 1.0 CB B:CYS100 3.4 18.8 1.0 CB B:CYS97 3.4 17.9 1.0 N B:CYS97 3.5 15.3 1.0 CA B:CYS111 3.7 13.5 1.0 N B:CYS100 3.9 18.7 1.0 CA B:CYS97 3.9 17.3 1.0 N B:LEU112 3.9 14.7 1.0 N B:GLY98 4.0 17.9 1.0 N B:CYS103 4.2 14.4 1.0 CA B:CYS100 4.2 18.2 1.0 C B:CYS111 4.3 14.4 1.0 C B:CYS97 4.4 18.2 1.0 CA B:CYS103 4.4 14.9 1.0 N B:LYS99 4.5 20.1 1.0 C B:GLN96 4.6 14.3 1.0 N B:LYS113 4.8 16.1 1.0 CG B:LYS113 4.9 20.7 1.0 C B:CYS100 4.9 18.4 1.0 CA B:GLN96 4.9 13.6 1.0 O B:CYS100 5.0 17.5 1.0

J.K.Rubach, B.V.Plapp. Amino Acid Residues in the Nicotinamide Binding Site Contribute to Catalysis By Horse Liver Alcohol Dehydrogenase Biochemistry V. 42 2907 2003.
ISSN: ISSN 0006-2960
PubMed: 12627956
DOI: 10.1021/BI0272656