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Zinc in PDB 3uko: Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, Complex with Nadh

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

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

Protein crystallography data

The structure of Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, Complex with Nadh, PDB code: 3uko 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) 38.92 / 1.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.244, 92.244, 172.872, 90.00, 90.00, 120.00
R / Rfree (%) 18 / 23.4

Zinc Binding Sites:

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

Zinc binding site 1 out of 4 in 3uko

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Zinc binding site 1 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, 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 S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:20.8
occ:1.00
 SG A:CYS113 2.3 21.6 0.5
SG A:CYS102 2.3 22.5 1.0
SG A:CYS105 2.3 21.4 1.0
SG A:CYS99 2.4 21.3 1.0
SG A:CYS113 2.4 19.1 0.5
CB A:CYS113 3.2 22.3 0.5
CB A:CYS102 3.3 25.0 1.0
CB A:CYS113 3.4 20.7 0.5
CB A:CYS99 3.4 18.7 1.0
CB A:CYS105 3.4 19.6 1.0
N A:CYS99 3.6 20.3 1.0
CA A:CYS113 3.7 22.8 0.5
N A:CYS102 3.8 23.2 1.0
CA A:CYS113 3.8 21.6 0.5
CA A:CYS99 3.9 20.6 1.0
N A:ARG100 3.9 19.8 1.0
CA A:CYS102 4.1 25.0 1.0
N A:GLY114 4.2 33.9 1.0
N A:CYS105 4.2 24.2 1.0
C A:CYS99 4.3 19.3 1.0
C A:CYS113 4.4 25.9 0.5
C A:CYS113 4.4 26.3 0.5
CA A:CYS105 4.4 21.5 1.0
N A:GLU101 4.4 21.8 1.0
CB A:LYS115 4.5 26.3 1.0
N A:LYS115 4.7 25.5 1.0
C A:GLU98 4.7 21.1 1.0
C A:CYS102 4.8 26.1 1.0
CA A:ARG100 4.9 20.4 1.0
N A:CYS113 4.9 25.5 0.5
O A:CYS102 4.9 25.6 1.0
C A:GLU101 4.9 23.3 1.0

Zinc binding site 2 out of 4 in 3uko

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Zinc binding site 2 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, 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 S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:28.0
occ:1.00
 OE2 A:GLU70 2.1 31.1 1.0
NE2 A:HIS69 2.1 21.9 1.0
SG A:CYS177 2.3 31.3 1.0
SG A:CYS47 2.3 27.7 1.0
CE1 A:HIS69 3.0 22.6 1.0
CD A:GLU70 3.0 29.1 1.0
CD2 A:HIS69 3.1 25.9 1.0
CB A:CYS177 3.2 27.5 1.0
CG A:GLU70 3.4 30.9 1.0
CB A:CYS47 3.4 30.7 1.0
NH2 A:ARG372 3.9 30.2 1.0
O A:HOH415 3.9 43.5 1.0
OE1 A:GLU70 4.1 26.8 1.0
ND1 A:HIS69 4.1 26.4 1.0
CG A:HIS69 4.2 25.6 1.0
OG1 A:THR49 4.5 28.6 1.0
CZ A:ARG372 4.5 27.0 1.0
CB A:THR49 4.6 25.7 1.0
NE A:ARG372 4.6 28.7 1.0
CA A:CYS47 4.7 30.1 1.0
CA A:CYS177 4.7 24.9 1.0
N A:CYS47 4.8 28.6 1.0
CB A:GLU70 4.8 28.7 1.0
N A:GLY178 4.9 27.1 1.0
O A:HOH437 4.9 22.0 1.0

Zinc binding site 3 out of 4 in 3uko

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Zinc binding site 3 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, 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 S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn400

b:21.5
occ:1.00
 SG B:CYS99 2.3 21.7 1.0
SG B:CYS113 2.3 21.1 0.5
SG B:CYS113 2.3 21.0 0.5
SG B:CYS102 2.3 22.3 1.0
SG B:CYS105 2.3 18.4 1.0
CB B:CYS113 3.2 23.7 0.5
CB B:CYS105 3.3 23.2 1.0
CB B:CYS99 3.3 17.7 1.0
CB B:CYS113 3.4 22.7 0.5
CB B:CYS102 3.4 23.0 1.0
N B:CYS99 3.6 18.5 1.0
O B:CYS113 3.8 39.6 0.5
CA B:CYS113 3.8 24.9 0.5
CA B:CYS99 3.9 20.4 1.0
C B:CYS113 3.9 23.9 0.5
N B:CYS102 3.9 24.2 1.0
CA B:CYS113 3.9 25.5 0.5
N B:ARG100 4.0 18.0 1.0
N B:CYS105 4.2 21.7 1.0
CA B:CYS102 4.2 22.9 1.0
C B:CYS99 4.3 21.6 1.0
CA B:CYS105 4.3 20.8 1.0
CB B:LYS115 4.4 19.5 0.5
N B:GLU101 4.4 22.9 1.0
N B:LYS115 4.5 26.4 0.5
CA B:GLY114 4.5 29.9 0.5
CB B:LYS115 4.6 24.4 0.5
N B:GLY114 4.7 28.2 0.5
C B:GLU98 4.7 19.1 1.0
C B:CYS102 4.9 23.6 1.0
C B:CYS113 4.9 22.3 0.5
O B:CYS102 4.9 24.0 1.0
CA B:ARG100 5.0 20.8 1.0
N B:CYS113 5.0 22.8 0.5
N B:LYS115 5.0 23.5 0.5

Zinc binding site 4 out of 4 in 3uko

Go back to Zinc Binding Sites List in 3uko
Zinc binding site 4 out of 4 in the Crystal Structure of S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, 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 S-Nitrosoglutathione Reductase From Arabidopsis Thaliana, Complex with Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:24.7
occ:1.00
 NE2 B:HIS69 2.0 18.6 1.0
OE2 B:GLU70 2.0 24.8 1.0
SG B:CYS47 2.2 24.2 1.0
SG B:CYS177 2.3 29.0 1.0
CE1 B:HIS69 3.0 19.6 1.0
CD B:GLU70 3.1 23.9 1.0
CD2 B:HIS69 3.1 18.1 1.0
CB B:CYS177 3.2 24.2 1.0
CB B:CYS47 3.3 24.8 1.0
CG B:GLU70 3.4 20.3 1.0
NH2 B:ARG372 3.8 23.2 1.0
ND1 B:HIS69 4.1 18.0 1.0
CG B:HIS69 4.2 20.5 1.0
OE1 B:GLU70 4.2 23.4 1.0
O B:HOH541 4.3 34.1 1.0
OG1 B:THR49 4.4 31.5 1.0
CA B:CYS47 4.6 25.5 1.0
CA B:CYS177 4.7 23.5 1.0
CB B:THR49 4.7 27.7 1.0
CZ B:ARG372 4.7 20.3 1.0
N B:GLY178 4.8 23.7 1.0
N B:CYS47 4.8 23.2 1.0
CB B:GLU70 4.9 17.6 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 Thaliana To Be Published.
Page generated: Wed Dec 16 04:54:57 2020

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