Zinc in PDB 1hsz: Human Beta-1 Alcohol Dehydrogenase (ADH1B*1)

All present enzymatic activity of Human Beta-1 Alcohol Dehydrogenase (ADH1B*1):
1.1.1.1;

The structure of Human Beta-1 Alcohol Dehydrogenase (ADH1B*1), PDB code: 1hsz was solved by M.S.Niederhut, B.J.Gibbons, S.Perez-Miller, T.D.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.00 / 2.20
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.900, 53.400, 90.200, 79.90, 89.50, 69.30
R / Rfree (%)	19.3 / 25.7

The binding sites of Zinc atom in the Human Beta-1 Alcohol Dehydrogenase (ADH1B*1) (pdb code 1hsz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Beta-1 Alcohol Dehydrogenase (ADH1B*1), PDB code: 1hsz:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Beta-1 Alcohol Dehydrogenase (ADH1B*1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Beta-1 Alcohol Dehydrogenase (ADH1B*1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1375 b:21.2 occ:1.00 SG A:CYS103 2.2 16.7 1.0 SG A:CYS100 2.3 18.5 1.0 SG A:CYS97 2.4 18.1 1.0 SG A:CYS111 2.4 21.9 1.0 CB A:CYS103 3.3 21.2 1.0 CB A:CYS97 3.4 21.1 1.0 CB A:CYS111 3.4 17.2 1.0 CB A:CYS100 3.5 19.6 1.0 N A:CYS97 3.6 15.9 1.0 N A:CYS100 3.7 20.4 1.0 CA A:CYS111 3.8 14.5 1.0 N A:GLY98 3.8 20.3 1.0 CA A:CYS97 3.9 17.9 1.0 N A:LEU112 4.0 17.8 1.0 N A:CYS103 4.2 18.2 1.0 CA A:CYS100 4.2 19.7 1.0 N A:LYS99 4.3 22.5 1.0 C A:CYS97 4.3 18.8 1.0 CA A:CYS103 4.3 19.5 1.0 C A:CYS111 4.3 17.9 1.0 C A:GLN96 4.6 14.1 1.0 CA A:GLY98 4.8 19.4 1.0 N A:LYS113 4.8 19.5 1.0 C A:CYS100 4.8 15.8 1.0 CG A:LYS113 4.8 22.7 1.0 C A:LYS99 4.9 23.6 1.0 CA A:GLN96 4.9 16.8 1.0 O A:CYS100 4.9 15.3 1.0 C A:GLY98 5.0 21.7 1.0

Zinc binding site 2 out of 4 in the Human Beta-1 Alcohol Dehydrogenase (ADH1B*1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Beta-1 Alcohol Dehydrogenase (ADH1B*1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1376 b:22.1 occ:1.00 O A:HOH1465 1.9 21.1 1.0 NE2 A:HIS67 2.2 20.1 1.0 SG A:CYS174 2.3 17.7 1.0 SG A:CYS46 2.4 20.8 1.0 CD2 A:HIS67 3.1 18.8 1.0 CE1 A:HIS67 3.2 14.2 1.0 CB A:CYS46 3.2 17.3 1.0 C5N A:NAD1377 3.3 18.8 1.0 CB A:CYS174 3.5 18.6 1.0 C6N A:NAD1377 3.9 20.1 1.0 C4N A:NAD1377 4.2 18.0 1.0 CB A:THR48 4.2 16.7 1.0 OG1 A:THR48 4.2 21.2 1.0 O A:HOH1379 4.2 23.4 1.0 CG A:HIS67 4.3 17.9 1.0 ND1 A:HIS67 4.3 15.1 1.0 NH2 A:ARG369 4.5 13.7 1.0 OE2 A:GLU68 4.7 20.0 1.0 CA A:CYS46 4.7 17.2 1.0 N A:GLY175 4.8 26.2 1.0 CA A:CYS174 4.8 22.0 1.0 CG2 A:THR48 5.0 15.9 1.0 C A:CYS174 5.0 24.3 1.0

Zinc binding site 3 out of 4 in the Human Beta-1 Alcohol Dehydrogenase (ADH1B*1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Beta-1 Alcohol Dehydrogenase (ADH1B*1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2375 b:16.9 occ:1.00 SG B:CYS103 2.3 18.5 1.0 SG B:CYS111 2.3 14.5 1.0 SG B:CYS100 2.3 17.2 1.0 SG B:CYS97 2.3 15.9 1.0 CB B:CYS97 3.2 18.5 1.0 CB B:CYS111 3.2 17.6 1.0 N B:CYS97 3.4 16.1 1.0 CB B:CYS100 3.4 16.1 1.0 CB B:CYS103 3.5 18.6 1.0 CA B:CYS111 3.7 16.0 1.0 CA B:CYS97 3.8 18.3 1.0 N B:GLY98 3.8 16.3 1.0 N B:LEU112 3.9 11.2 1.0 N B:CYS100 4.0 15.0 1.0 C B:CYS97 4.2 16.7 1.0 C B:CYS111 4.2 12.8 1.0 N B:CYS103 4.3 14.5 1.0 CA B:CYS100 4.3 16.4 1.0 CA B:CYS103 4.4 15.6 1.0 C B:GLN96 4.5 17.3 1.0 N B:LYS99 4.6 18.9 1.0 CG B:LYS113 4.8 20.1 1.0 NZ B:LYS113 4.8 33.3 1.0 CA B:GLN96 4.8 14.8 1.0 O B:CYS100 4.8 13.9 1.0 N B:LYS113 4.8 19.0 1.0 C B:CYS100 4.8 14.8 1.0 CA B:GLY98 4.8 15.8 1.0 N B:CYS111 5.0 18.4 1.0

Zinc binding site 4 out of 4 in the Human Beta-1 Alcohol Dehydrogenase (ADH1B*1)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Beta-1 Alcohol Dehydrogenase (ADH1B*1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2376 b:23.3 occ:1.00 SG B:CYS174 2.1 17.3 1.0 NE2 B:HIS67 2.1 13.6 1.0 SG B:CYS46 2.3 21.2 1.0 O B:HOH2379 2.8 23.5 1.0 CD2 B:HIS67 3.0 13.1 1.0 CE1 B:HIS67 3.2 13.6 1.0 C5N B:NAD2377 3.2 25.6 1.0 CB B:CYS46 3.3 20.7 1.0 CB B:CYS174 3.3 18.2 1.0 OG1 B:THR48 3.8 21.4 1.0 C6N B:NAD2377 3.9 27.7 1.0 C4N B:NAD2377 4.0 24.1 1.0 CB B:THR48 4.1 22.1 1.0 CG B:HIS67 4.2 14.0 1.0 ND1 B:HIS67 4.3 15.2 1.0 NH2 B:ARG369 4.6 13.8 1.0 N B:GLY175 4.6 20.3 1.0 CA B:CYS174 4.6 21.1 1.0 OE2 B:GLU68 4.6 29.4 1.0 CA B:CYS46 4.7 19.2 1.0 C B:CYS174 4.9 18.4 1.0 N B:THR48 5.0 16.6 1.0

M.S.Niederhut, B.J.Gibbons, S.Perez-Miller, T.D.Hurley. Three-Dimensional Structures of the Three Human Class I Alcohol Dehydrogenases. Protein Sci. V. 10 697 2001.
ISSN: ISSN 0961-8368
PubMed: 11274460
DOI: 10.1110/PS.45001