Zinc in PDB 4rqt: Alcohol Dehydrogenase Crystal Structure

All present enzymatic activity of Alcohol Dehydrogenase Crystal Structure:
1.1.1.1;

The structure of Alcohol Dehydrogenase Crystal Structure, PDB code: 4rqt was solved by Y.W.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.51 / 2.30
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	103.604, 103.604, 168.127, 90.00, 90.00, 120.00
R / Rfree (%)	16.2 / 20.1

The binding sites of Zinc atom in the Alcohol Dehydrogenase Crystal Structure (pdb code 4rqt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Alcohol Dehydrogenase Crystal Structure, PDB code: 4rqt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Alcohol Dehydrogenase Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Alcohol Dehydrogenase Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:32.5 occ:1.00 SG A:CYS105 2.3 30.8 1.0 SG A:CYS99 2.3 32.9 1.0 SG A:CYS113 2.4 27.8 1.0 SG A:CYS102 2.4 29.1 1.0 H A:CYS99 2.8 47.9 1.0 HA A:CYS113 3.1 29.9 1.0 H A:GLY100 3.1 50.5 1.0 H A:CYS102 3.1 52.2 1.0 HB2 A:CYS105 3.1 41.8 1.0 HB3 A:CYS102 3.2 35.3 1.0 HB2 A:CYS113 3.2 29.5 1.0 CB A:CYS113 3.2 24.6 1.0 HB3 A:CYS99 3.3 45.2 1.0 CB A:CYS99 3.3 37.7 1.0 CB A:CYS105 3.3 34.8 1.0 CB A:CYS102 3.4 29.4 1.0 N A:CYS99 3.5 39.9 1.0 H A:ASP114 3.5 29.9 1.0 H A:CYS105 3.6 36.4 1.0 CA A:CYS113 3.6 25.0 1.0 H A:GLU101 3.7 57.0 1.0 N A:GLY100 3.7 42.0 1.0 H A:LEU115 3.8 42.0 1.0 N A:CYS102 3.8 43.5 1.0 CA A:CYS99 3.8 33.9 1.0 HB3 A:CYS105 4.0 41.8 1.0 N A:ASP114 4.0 24.9 1.0 HB3 A:CYS113 4.1 29.5 1.0 HA A:GLU98 4.1 28.5 1.0 HB2 A:CYS102 4.1 35.3 1.0 CA A:CYS102 4.2 33.4 1.0 HB2 A:CYS99 4.2 45.2 1.0 C A:CYS99 4.2 39.6 1.0 N A:CYS105 4.2 30.3 1.0 C A:CYS113 4.2 27.1 1.0 HB3 A:LEU115 4.3 36.8 1.0 CA A:CYS105 4.4 31.1 1.0 N A:GLU101 4.4 47.5 1.0 C A:GLU98 4.5 31.8 1.0 HB2 A:LEU115 4.5 36.8 1.0 N A:LEU115 4.6 35.0 1.0 HA A:CYS105 4.7 37.3 1.0 HB2 A:HIS104 4.7 31.5 1.0 CA A:GLY100 4.8 45.2 1.0 HA A:CYS99 4.8 40.6 1.0 HB2 A:ASP114 4.8 34.2 1.0 CA A:GLU98 4.8 23.7 1.0 C A:CYS102 4.8 27.3 1.0 N A:CYS113 4.9 27.7 1.0 HA2 A:GLY100 4.9 54.2 1.0 CB A:LEU115 4.9 30.7 1.0 H A:LEU116 4.9 37.8 1.0 O A:HOH586 4.9 41.4 1.0 C A:GLU101 5.0 47.0 1.0 O A:HOH665 5.0 45.2 1.0 HA A:CYS102 5.0 40.1 1.0 C A:GLY100 5.0 49.9 1.0

Zinc binding site 2 out of 2 in the Alcohol Dehydrogenase Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Alcohol Dehydrogenase Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:32.9 occ:1.00 NE2 A:HIS69 2.1 28.3 1.0 O A:ACY406 2.2 31.3 1.0 SG A:CYS177 2.3 29.6 1.0 SG A:CYS47 2.3 22.7 1.0 H1 A:ACY406 3.0 42.7 1.0 CE1 A:HIS69 3.0 20.4 1.0 CD2 A:HIS69 3.1 17.6 1.0 C A:ACY406 3.2 40.9 1.0 HE1 A:HIS69 3.2 24.5 1.0 HB A:THR49 3.3 29.9 1.0 HD2 A:HIS69 3.3 21.2 1.0 HB3 A:CYS47 3.3 26.8 1.0 CB A:CYS47 3.3 22.4 1.0 HB3 A:CYS177 3.3 36.2 1.0 HB2 A:CYS47 3.4 26.8 1.0 CB A:CYS177 3.4 30.2 1.0 CH3 A:ACY406 3.6 35.6 1.0 O A:HOH657 3.6 51.1 1.0 HB2 A:CYS177 3.6 36.2 1.0 OG1 A:THR49 4.0 25.7 1.0 H3 A:ACY406 4.0 42.7 1.0 CB A:THR49 4.0 24.9 1.0 ND1 A:HIS69 4.2 22.9 1.0 HG3 A:GLU70 4.2 42.9 1.0 CG A:HIS69 4.2 22.0 1.0 H A:THR49 4.2 22.8 1.0 OE2 A:GLU70 4.3 28.9 1.0 OXT A:ACY406 4.3 42.1 1.0 H A:GLY178 4.4 40.8 1.0 H2 A:ACY406 4.5 42.7 1.0 HG23 A:THR49 4.6 35.3 1.0 HH21 A:ARG372 4.7 23.1 1.0 N A:GLY178 4.7 34.0 1.0 CA A:CYS177 4.7 30.2 1.0 CA A:CYS47 4.8 17.1 1.0 HG1 A:THR49 4.8 30.9 1.0 HA2 A:GLY178 4.8 45.9 1.0 CG A:GLU70 4.9 35.8 1.0 CG2 A:THR49 4.9 29.4 1.0 HG2 A:GLU70 4.9 42.9 1.0 HD1 A:HIS69 4.9 27.5 1.0 N A:THR49 5.0 19.0 1.0 CD A:GLU70 5.0 34.4 1.0

F.Chen, P.Wang, Y.An, J.Huang, Y.Xu. Structural Insight Into the Conformational Change of Alcohol Dehydrogenase From Arabidopsis Thalianal During Coenzyme Binding. Biochimie V.108C 33 2014.
ISSN: ISSN 0300-9084
PubMed: 25447145
DOI: 10.1016/J.BIOCHI.2014.10.023