Zinc in PDB 1hso: Human Alpha Alcohol Dehydrogenase (ADH1A)

All present enzymatic activity of Human Alpha Alcohol Dehydrogenase (ADH1A):
1.1.1.1;

The structure of Human Alpha Alcohol Dehydrogenase (ADH1A), PDB code: 1hso 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 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.700, 100.200, 69.100, 90.00, 104.90, 90.00
R / Rfree (%)	24.8 / 19.1

The structure of Human Alpha Alcohol Dehydrogenase (ADH1A) also contains other interesting chemical elements:

Iodine

(I)

2 atoms

The binding sites of Zinc atom in the Human Alpha Alcohol Dehydrogenase (ADH1A) (pdb code 1hso). 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 Alpha Alcohol Dehydrogenase (ADH1A), PDB code: 1hso:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Alpha Alcohol Dehydrogenase (ADH1A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Alpha Alcohol Dehydrogenase (ADH1A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1375 b:27.4 occ:1.00 SG A:CYS97 2.2 19.5 1.0 SG A:CYS111 2.3 24.9 1.0 SG A:CYS100 2.3 13.7 1.0 SG A:CYS103 2.4 21.9 1.0 CB A:CYS111 3.2 11.7 1.0 CB A:CYS100 3.3 18.3 1.0 CB A:CYS103 3.3 17.0 1.0 CB A:CYS97 3.4 19.4 1.0 N A:CYS97 3.5 18.1 1.0 CA A:CYS111 3.8 19.2 1.0 N A:GLY98 3.8 21.8 1.0 N A:CYS100 3.9 19.5 1.0 CA A:CYS97 3.9 22.7 1.0 N A:LEU112 3.9 22.1 1.0 CA A:CYS100 4.2 19.1 1.0 N A:CYS103 4.2 16.3 1.0 C A:CYS97 4.3 22.1 1.0 C A:CYS111 4.3 20.8 1.0 CA A:CYS103 4.3 17.3 1.0 N A:LYS99 4.4 17.3 1.0 C A:GLN96 4.4 13.7 1.0 CA A:GLN96 4.8 14.4 1.0 CA A:GLY98 4.8 21.5 1.0 N A:LYS113 4.8 17.3 1.0 C A:LYS99 4.9 18.3 1.0 C A:CYS100 4.9 18.0 1.0

Zinc binding site 2 out of 4 in the Human Alpha Alcohol Dehydrogenase (ADH1A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Alpha Alcohol Dehydrogenase (ADH1A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1376 b:24.7 occ:1.00 NE2 A:HIS67 2.1 16.1 1.0 SG A:CYS174 2.2 16.9 1.0 O A:HOH467 2.2 19.5 1.0 SG A:CYS46 2.4 12.8 1.0 CD2 A:HIS67 3.1 18.0 1.0 CE1 A:HIS67 3.1 18.5 1.0 C5N A:NAD1377 3.2 10.1 1.0 CB A:CYS46 3.3 7.4 1.0 CB A:CYS174 3.5 9.8 1.0 C6N A:NAD1377 3.8 7.6 1.0 OG1 A:THR48 3.8 17.6 1.0 CB A:THR48 3.9 18.6 1.0 C4N A:NAD1377 4.0 11.4 1.0 ND1 A:HIS67 4.3 21.9 1.0 CG A:HIS67 4.3 18.6 1.0 CG2 A:THR48 4.7 14.4 1.0 CA A:CYS46 4.7 8.3 1.0 N A:THR48 4.8 13.3 1.0 CA A:CYS174 4.8 13.2 1.0 N1N A:NAD1377 4.9 5.2 1.0 OE2 A:GLU68 5.0 11.7 1.0

Zinc binding site 3 out of 4 in the Human Alpha Alcohol Dehydrogenase (ADH1A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Alpha Alcohol Dehydrogenase (ADH1A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2375 b:28.9 occ:1.00 SG B:CYS103 2.2 16.3 1.0 SG B:CYS97 2.3 28.0 1.0 SG B:CYS100 2.3 23.3 1.0 SG B:CYS111 2.3 26.0 1.0 CB B:CYS103 3.1 22.8 1.0 CB B:CYS111 3.2 17.5 1.0 CB B:CYS100 3.3 20.6 1.0 N B:CYS97 3.4 28.1 1.0 CB B:CYS97 3.5 23.0 1.0 N B:GLY98 3.7 24.1 1.0 CA B:CYS111 3.8 19.5 1.0 CA B:CYS97 3.9 24.8 1.0 N B:CYS100 3.9 25.5 1.0 N B:LEU112 4.0 18.8 1.0 CA B:CYS100 4.2 24.3 1.0 N B:CYS103 4.2 17.1 1.0 C B:CYS97 4.2 26.2 1.0 CA B:CYS103 4.2 21.2 1.0 C B:GLN96 4.4 29.3 1.0 C B:CYS111 4.4 19.5 1.0 N B:LYS99 4.4 21.4 1.0 CA B:GLN96 4.6 27.2 1.0 CA B:GLY98 4.7 21.1 1.0 O B:CYS100 4.9 24.8 1.0 C B:CYS100 4.9 23.4 1.0 C B:GLY98 5.0 22.0 1.0 N B:LYS113 5.0 24.2 1.0 C B:LYS99 5.0 25.9 1.0

Zinc binding site 4 out of 4 in the Human Alpha Alcohol Dehydrogenase (ADH1A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Alpha Alcohol Dehydrogenase (ADH1A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2376 b:30.1 occ:1.00 NE2 B:HIS67 2.1 24.5 1.0 SG B:CYS174 2.1 25.7 1.0 O B:HOH723 2.4 35.0 1.0 SG B:CYS46 2.5 22.7 1.0 CD2 B:HIS67 3.0 25.6 1.0 CE1 B:HIS67 3.1 19.2 1.0 C5N B:NAD2377 3.3 22.2 1.0 CB B:CYS46 3.4 21.0 1.0 CB B:CYS174 3.4 28.3 1.0 C6N B:NAD2377 3.9 21.9 1.0 OG1 B:THR48 4.0 16.2 1.0 CB B:THR48 4.0 20.5 1.0 C4N B:NAD2377 4.0 23.9 1.0 CG B:HIS67 4.1 25.6 1.0 ND1 B:HIS67 4.2 22.2 1.0 CG2 B:THR48 4.7 27.3 1.0 CA B:CYS174 4.8 21.5 1.0 CA B:CYS46 4.9 19.8 1.0 N B:GLY175 4.9 17.5 1.0 N1N B:NAD2377 5.0 22.9 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