Zinc in PDB 4l0q: Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant

The structure of Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant, PDB code: 4l0q was solved by A.Weichsel, J.Crotty, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.65 / 1.95
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.731, 92.731, 173.558, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 25.1

The binding sites of Zinc atom in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant (pdb code 4l0q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant, PDB code: 4l0q:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:39.9 occ:1.00 SG A:CYS105 2.3 39.8 1.0 SG A:CYS99 2.4 36.4 1.0 SG A:CYS113 2.4 40.9 1.0 SG A:CYS102 2.4 39.1 1.0 CB A:CYS113 3.2 42.5 1.0 CB A:CYS99 3.4 43.6 1.0 CB A:CYS105 3.4 42.8 1.0 N A:CYS99 3.5 39.0 1.0 CB A:CYS102 3.5 38.0 1.0 N A:ARG100 3.8 36.2 1.0 CA A:CYS113 3.8 42.2 1.0 N A:CYS102 3.8 42.4 1.0 CA A:CYS99 3.9 39.1 1.0 C A:CYS99 4.2 41.7 1.0 CA A:CYS102 4.2 40.7 1.0 N A:CYS105 4.3 43.3 1.0 N A:GLY114 4.3 49.5 1.0 N A:GLU101 4.3 43.4 1.0 C A:CYS113 4.4 43.2 1.0 CA A:CYS105 4.4 40.3 1.0 CB A:LYS115 4.4 48.3 1.0 C A:GLU98 4.6 37.5 1.0 N A:LYS115 4.7 48.9 1.0 CA A:ARG100 4.8 39.1 1.0 C A:GLU101 4.9 47.2 1.0 C A:CYS102 4.9 41.1 1.0 CA A:GLU98 4.9 35.4 1.0 O A:CYS102 4.9 41.2 1.0 C A:ARG100 5.0 43.1 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:44.1 occ:1.00 OE2 A:GLU70 2.0 47.6 1.0 NE2 A:HIS69 2.1 32.2 1.0 SG A:CYS47 2.2 39.5 1.0 SG A:CYS177 2.4 44.2 1.0 CE1 A:HIS69 2.9 34.0 1.0 CD A:GLU70 3.1 44.7 1.0 CD2 A:HIS69 3.1 34.1 1.0 CB A:CYS177 3.1 41.4 1.0 CB A:CYS47 3.3 41.8 1.0 CG A:GLU70 3.4 43.5 1.0 NH2 A:ARG372 3.8 35.2 1.0 ND1 A:HIS69 4.1 32.1 1.0 OE1 A:GLU70 4.2 37.5 1.0 O A:HOH594 4.2 38.8 1.0 CG A:HIS69 4.2 34.9 1.0 OG1 A:THR49 4.4 33.0 1.0 CA A:CYS47 4.4 41.0 1.0 N A:CYS47 4.5 42.9 1.0 CB A:THR49 4.5 41.2 1.0 CA A:CYS177 4.6 40.1 1.0 CZ A:ARG372 4.6 38.6 1.0 N A:GLY178 4.7 37.2 1.0 O A:HOH527 4.8 37.5 1.0 C5N A:NAD403 4.9 45.7 1.0 NE A:ARG372 4.9 42.1 1.0 CB A:GLU70 4.9 39.2 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:48.4 occ:1.00 SG B:CYS105 2.4 49.7 1.0 SG B:CYS99 2.4 47.7 1.0 SG B:CYS113 2.5 49.5 1.0 SG B:CYS102 2.6 46.1 1.0 CB B:CYS113 3.2 52.4 1.0 CB B:CYS105 3.3 49.1 1.0 CB B:CYS99 3.3 43.6 1.0 CB B:CYS102 3.5 52.8 1.0 N B:CYS99 3.5 44.5 1.0 CA B:CYS113 3.8 63.2 1.0 CA B:CYS99 3.9 48.5 1.0 N B:ARG100 3.9 45.4 1.0 N B:CYS102 3.9 60.9 1.0 N B:CYS105 4.3 51.9 1.0 C B:CYS99 4.3 48.0 1.0 CB B:LYS115 4.3 58.9 1.0 CA B:CYS102 4.3 55.2 1.0 N B:GLY114 4.3 73.8 1.0 CA B:CYS105 4.3 52.3 1.0 C B:CYS113 4.4 60.8 1.0 N B:GLU101 4.4 57.3 1.0 N B:LYS115 4.6 64.1 1.0 C B:GLU98 4.7 44.0 1.0 CA B:ARG100 4.8 49.9 1.0 C B:CYS102 4.9 60.3 1.0 O B:CYS102 5.0 53.5 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, C370A/C373A Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:34.0 occ:1.00 OE2 B:GLU70 2.0 33.8 1.0 NE2 B:HIS69 2.2 35.6 1.0 SG B:CYS47 2.3 31.7 1.0 SG B:CYS177 2.3 36.0 1.0 CE1 B:HIS69 2.9 32.8 1.0 CD B:GLU70 3.1 35.8 1.0 CB B:CYS177 3.2 35.4 1.0 CD2 B:HIS69 3.3 35.8 1.0 CB B:CYS47 3.4 32.4 1.0 CG B:GLU70 3.4 33.0 1.0 NH2 B:ARG372 3.8 29.9 1.0 ND1 B:HIS69 4.1 31.7 1.0 O B:HOH574 4.1 34.9 1.0 OE1 B:GLU70 4.2 34.0 1.0 CG B:HIS69 4.3 29.4 1.0 CA B:CYS47 4.5 36.0 1.0 N B:CYS47 4.6 38.9 1.0 OG1 B:THR49 4.6 39.4 1.0 CB B:THR49 4.6 34.0 1.0 CA B:CYS177 4.7 34.1 1.0 CZ B:ARG372 4.7 37.1 1.0 C5N B:NAD403 4.8 58.6 1.0 N B:GLY178 4.8 31.2 1.0 CB B:GLU70 4.9 36.5 1.0 NE B:ARG372 5.0 30.9 1.0

J.Crotty, M.Greving, S.Brettschneider, A.Weichsel, G.F.Wildner, E.Vierling, W.R.Montfort. Crystal Structure and Kinetic Behavior of Alcohol Dehydrogenase III/S-Nitrosoglutathione Reductase From Arabidopsis Thaliana To Be Published.