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Zinc in PDB 4gl4: Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh

Enzymatic activity of Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh

All present enzymatic activity of Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh:
1.1.1.1; 1.1.1.284;

Protein crystallography data

The structure of Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh, PDB code: 4gl4 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) 27.13 / 1.80
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.634, 91.634, 173.184, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 23.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh (pdb code 4gl4). 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 Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh, PDB code: 4gl4:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4gl4

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Zinc binding site 1 out of 4 in the Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh


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 Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:32.2
occ:1.00
 SG A:CYS105 2.3 33.5 1.0
SG A:CYS113 2.3 30.1 1.0
SG A:CYS102 2.4 34.2 1.0
SG A:CYS99 2.4 33.8 1.0
CB A:CYS113 3.2 33.1 1.0
CB A:CYS99 3.3 33.7 1.0
CB A:CYS102 3.4 32.3 1.0
CB A:CYS105 3.4 34.1 1.0
N A:CYS99 3.5 30.7 1.0
CA A:CYS113 3.7 36.1 1.0
N A:ARG100 3.8 33.2 1.0
CA A:CYS99 3.8 34.9 1.0
N A:CYS102 3.8 36.4 1.0
C A:CYS99 4.1 34.1 1.0
CA A:CYS102 4.2 34.0 1.0
N A:CYS105 4.2 35.4 1.0
C A:CYS113 4.4 40.8 1.0
CA A:CYS105 4.4 36.0 1.0
N A:GLY114 4.4 45.1 1.0
N A:GLU101 4.4 33.5 1.0
CB A:LYS115 4.4 37.0 1.0
C A:GLU98 4.6 33.0 1.0
N A:LYS115 4.7 39.1 1.0
CA A:ARG100 4.8 35.0 1.0
C A:CYS102 4.9 36.0 1.0
C A:GLU101 4.9 37.7 1.0
O A:CYS102 4.9 36.5 1.0
CA A:GLU98 5.0 29.6 1.0

Zinc binding site 2 out of 4 in 4gl4

Go back to Zinc Binding Sites List in 4gl4
Zinc binding site 2 out of 4 in the Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh


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 Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:39.9
occ:1.00
 OE2 A:GLU70 2.2 48.3 1.0
NE2 A:HIS69 2.2 34.9 1.0
SG A:CYS177 2.3 49.2 1.0
SG A:CYS47 2.3 42.0 1.0
CE1 A:HIS69 2.8 38.1 1.0
CB A:CYS177 3.1 41.2 1.0
CD A:GLU70 3.2 41.1 1.0
CD2 A:HIS69 3.3 32.3 1.0
CB A:CYS47 3.3 41.2 1.0
CG A:GLU70 3.5 41.3 1.0
NH2 A:ARG372 3.9 43.9 1.0
ND1 A:HIS69 4.0 33.4 1.0
CG A:HIS69 4.3 31.2 1.0
OE1 A:GLU70 4.3 39.7 1.0
OG1 A:THR49 4.3 36.2 1.0
CB A:THR49 4.5 35.5 1.0
CA A:CYS47 4.6 39.8 1.0
CA A:CYS177 4.6 35.3 1.0
CZ A:ARG372 4.6 45.8 1.0
NE A:ARG372 4.7 42.5 1.0
N A:CYS47 4.8 40.0 1.0
O A:HOH545 4.8 33.0 1.0
N A:GLY178 4.8 33.4 1.0
CB A:GLU70 4.9 36.4 1.0
OD2 A:ASP50 4.9 33.2 1.0

Zinc binding site 3 out of 4 in 4gl4

Go back to Zinc Binding Sites List in 4gl4
Zinc binding site 3 out of 4 in the Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh


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 Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:27.9
occ:0.70
 SG B:CYS99 2.2 36.7 1.0
SG B:CYS102 2.4 37.4 1.0
SG B:CYS113 2.4 39.6 1.0
SG B:CYS105 2.5 36.3 1.0
CB B:CYS113 3.1 44.6 1.0
CB B:CYS99 3.3 36.0 1.0
CB B:CYS105 3.4 40.4 1.0
CB B:CYS102 3.4 43.3 1.0
N B:CYS99 3.6 34.6 1.0
CA B:CYS113 3.7 52.6 1.0
N B:CYS102 3.9 47.2 1.0
N B:ARG100 3.9 34.9 1.0
CA B:CYS99 3.9 35.3 1.0
CA B:CYS102 4.2 44.1 1.0
N B:GLY114 4.2 64.3 1.0
N B:CYS105 4.2 40.3 1.0
C B:CYS99 4.3 36.9 1.0
C B:CYS113 4.4 55.3 1.0
CA B:CYS105 4.4 40.5 1.0
N B:GLU101 4.4 44.2 1.0
CB B:LYS115 4.6 52.7 1.0
N B:LYS115 4.7 52.8 1.0
C B:GLU98 4.8 32.4 1.0
OD1 B:ASN111 4.8 74.0 1.0
C B:CYS102 4.9 43.8 1.0
N B:CYS113 4.9 56.3 1.0
CA B:ARG100 4.9 40.1 1.0

Zinc binding site 4 out of 4 in 4gl4

Go back to Zinc Binding Sites List in 4gl4
Zinc binding site 4 out of 4 in the Crystal Structure of Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh


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 Oxidized S-Nitrosoglutathione Reductase From Arabidopsis Thalina, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:32.9
occ:1.00
 OE2 B:GLU70 2.1 30.5 1.0
NE2 B:HIS69 2.2 26.1 1.0
SG B:CYS47 2.3 30.4 1.0
SG B:CYS177 2.4 39.7 1.0
CB B:CYS47 2.9 30.5 1.0
CE1 B:HIS69 3.0 24.6 1.0
CD2 B:HIS69 3.2 24.7 1.0
CD B:GLU70 3.2 35.6 1.0
CB B:CYS177 3.3 36.2 1.0
O B:HOH654 3.6 52.5 1.0
CG B:GLU70 3.6 30.2 1.0
NH2 B:ARG372 3.9 38.9 1.0
ND1 B:HIS69 4.2 25.4 1.0
CG B:HIS69 4.3 21.7 1.0
OE1 B:GLU70 4.4 34.7 1.0
CA B:CYS47 4.4 32.8 1.0
OG1 B:THR49 4.5 35.5 1.0
CB B:THR49 4.7 29.8 1.0
CA B:CYS177 4.8 29.3 1.0
CZ B:ARG372 4.8 37.0 1.0
N B:GLY178 4.9 27.9 1.0

Reference:

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 Thalina To Be Published.
Page generated: Sat Oct 26 23:21:16 2024

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