Zinc in PDB 8co4: Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina

Enzymatic activity of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina

All present enzymatic activity of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina:
1.1.1.1; 1.1.1.284;

Protein crystallography data

The structure of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina, PDB code: 8co4 was solved by S.Fermani, S.Fanti, G.Carloni, J.Rossi, G.Falini, M.Zaffagnini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.92 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 88.6, 93.927, 167.484, 90, 90, 90
R / Rfree (%) 16.1 / 21.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina (pdb code 8co4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina, PDB code: 8co4:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 1 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


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 Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:21.0
occ:0.99
 SG A:CYS105 2.3 22.1 1.0
SG A:CYS113 2.3 21.7 1.0
SG A:CYS99 2.4 21.4 1.0
SG A:CYS102 2.4 21.9 1.0
CB A:CYS113 3.2 19.8 1.0
CB A:CYS105 3.3 22.9 1.0
CB A:CYS102 3.4 24.8 1.0
CB A:CYS99 3.4 24.4 1.0
N A:CYS99 3.5 16.0 1.0
CA A:CYS113 3.7 22.8 1.0
N A:CYS102 3.8 20.8 1.0
CA A:CYS99 3.9 22.7 1.0
N A:ARG100 3.9 16.1 1.0
N A:GLY114 4.1 26.6 1.0
N A:CYS105 4.1 24.2 1.0
CA A:CYS102 4.2 26.2 1.0
C A:CYS113 4.3 31.3 1.0
C A:CYS99 4.3 24.4 1.0
CA A:CYS105 4.3 26.0 1.0
N A:GLU101 4.4 19.7 1.0
CB A:LYS115 4.5 24.4 1.0
N A:LYS115 4.5 29.8 1.0
C A:GLU98 4.7 21.3 1.0
C A:CYS102 4.9 23.7 1.0
CA A:ARG100 4.9 21.9 1.0
O A:LEU112 4.9 29.6 1.0
N A:CYS113 5.0 23.9 1.0
C A:GLU101 5.0 27.5 1.0

Zinc binding site 2 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 2 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


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 Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:39.8
occ:0.85
 O A:HOH504 1.6 23.9 1.0
O A:HOH658 1.6 33.4 1.0
NE2 A:HIS69 2.2 31.6 1.0
SG A:CYS177 2.3 37.5 1.0
SG A:CYS47 2.3 29.5 1.0
CD2 A:HIS69 3.1 25.8 1.0
CE1 A:HIS69 3.3 26.1 1.0
CB A:CYS177 3.3 36.5 1.0
CB A:CYS47 3.4 31.7 1.0
OE2 A:GLU70 3.7 33.5 1.0
CB A:THR49 4.0 32.4 1.0
OG1 A:THR49 4.0 30.3 1.0
CG A:HIS69 4.3 22.3 1.0
ND1 A:HIS69 4.3 21.6 1.0
CG A:GLU70 4.4 29.7 1.0
O A:HOH764 4.5 48.2 1.0
CD A:GLU70 4.5 32.8 1.0
NH2 A:ARG372 4.5 27.1 1.0
CA A:CYS177 4.7 23.6 1.0
CG2 A:THR49 4.8 28.3 1.0
N A:GLY178 4.8 26.5 1.0
CA A:CYS47 4.8 38.4 1.0
N A:THR49 5.0 25.1 1.0
C A:CYS177 5.0 24.8 1.0

Zinc binding site 3 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 3 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


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 Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:19.8
occ:0.97
 SG B:CYS105 2.3 21.5 1.0
SG B:CYS99 2.3 21.0 1.0
SG B:CYS102 2.4 19.5 1.0
SG B:CYS113 2.4 18.8 1.0
CB B:CYS113 3.2 22.0 1.0
CB B:CYS102 3.3 20.2 1.0
CB B:CYS105 3.3 25.0 1.0
CB B:CYS99 3.4 19.1 1.0
N B:CYS99 3.6 16.1 1.0
CA B:CYS113 3.7 23.4 1.0
N B:CYS102 3.7 21.5 1.0
CA B:CYS99 3.9 17.8 1.0
N B:ARG100 3.9 15.6 1.0
N B:GLY114 4.0 24.9 1.0
CA B:CYS102 4.1 25.9 1.0
N B:CYS105 4.1 17.1 1.0
C B:CYS113 4.2 24.7 1.0
C B:CYS99 4.3 19.6 1.0
N B:GLU101 4.3 26.4 1.0
CA B:CYS105 4.3 22.0 1.0
N B:LYS115 4.4 21.6 1.0
CB B:LYS115 4.4 18.3 1.0
C B:GLU98 4.7 15.5 1.0
C B:GLU101 4.9 28.6 1.0
C B:CYS102 4.9 19.6 1.0
CA B:ARG100 4.9 24.4 1.0
CA B:LYS115 5.0 16.1 1.0
N B:CYS113 5.0 20.7 1.0

Zinc binding site 4 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 4 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


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 Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:30.5
occ:0.90
 O B:HOH527 1.7 21.7 1.0
O B:HOH547 1.8 25.2 1.0
NE2 B:HIS69 2.2 34.5 1.0
SG B:CYS177 2.3 28.6 1.0
SG B:CYS47 2.3 27.2 1.0
CE1 B:HIS69 3.1 25.4 1.0
CD2 B:HIS69 3.3 28.4 1.0
CB B:CYS177 3.3 24.6 1.0
CB B:CYS47 3.4 27.6 1.0
OG1 B:THR49 3.9 26.6 1.0
CB B:THR49 4.0 23.0 1.0
OE2 B:GLU70 4.1 31.5 1.0
ND1 B:HIS69 4.2 25.0 1.0
CG B:HIS69 4.4 20.0 1.0
CG B:GLU70 4.7 26.8 1.0
CA B:CYS177 4.7 22.1 1.0
O B:HOH736 4.7 46.6 1.0
NH2 B:ARG372 4.7 23.3 1.0
CG2 B:THR49 4.8 27.3 1.0
CD B:GLU70 4.8 35.1 1.0
CA B:CYS47 4.9 30.3 1.0
N B:GLY178 4.9 26.1 1.0
N B:THR49 4.9 21.3 1.0

Zinc binding site 5 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 5 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:20.6
occ:1.00
 SG C:CYS99 2.3 20.9 1.0
SG C:CYS105 2.3 20.2 1.0
SG C:CYS113 2.4 18.7 1.0
SG C:CYS102 2.4 18.7 1.0
CB C:CYS113 3.2 20.9 1.0
CB C:CYS102 3.4 18.4 1.0
CB C:CYS99 3.4 14.6 1.0
CB C:CYS105 3.4 19.3 1.0
N C:CYS99 3.6 15.9 1.0
CA C:CYS113 3.7 21.0 1.0
N C:CYS102 3.7 17.9 1.0
N C:ARG100 3.9 20.4 1.0
CA C:CYS99 3.9 13.9 1.0
N C:GLY114 4.0 24.1 1.0
CA C:CYS102 4.1 19.6 1.0
N C:CYS105 4.2 18.1 1.0
C C:CYS99 4.3 20.7 1.0
C C:CYS113 4.3 29.9 1.0
N C:LYS115 4.3 17.7 1.0
CB C:LYS115 4.3 24.1 1.0
N C:GLU101 4.4 17.5 1.0
CA C:CYS105 4.4 18.3 1.0
C C:GLU98 4.7 15.7 1.0
C C:CYS102 4.8 19.6 1.0
CA C:ARG100 4.9 18.9 1.0
C C:GLU101 4.9 30.8 1.0
CA C:LYS115 4.9 25.1 1.0
O C:CYS102 4.9 19.7 1.0

Zinc binding site 6 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 6 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn402

b:25.2
occ:0.90
 O C:HOH531 1.7 26.9 1.0
O C:HOH558 1.9 28.8 1.0
NE2 C:HIS69 2.2 22.6 1.0
SG C:CYS177 2.3 25.6 1.0
SG C:CYS47 2.4 27.1 1.0
CE1 C:HIS69 3.1 24.9 1.0
CD2 C:HIS69 3.2 20.4 1.0
CB C:CYS177 3.4 25.2 1.0
CB C:CYS47 3.4 22.7 1.0
OG1 C:THR49 3.8 28.6 1.0
CB C:THR49 3.9 24.3 1.0
O C:HOH716 4.1 33.7 1.0
OE1 C:GLU70 4.2 33.7 1.0
O C:HOH741 4.2 36.7 1.0
ND1 C:HIS69 4.2 20.7 1.0
CG C:HIS69 4.3 15.2 1.0
CG2 C:THR49 4.7 25.6 1.0
CA C:CYS177 4.8 21.6 1.0
CG C:GLU70 4.8 30.2 1.0
N C:THR49 4.8 18.6 1.0
CE1 C:TYR95 4.8 27.6 1.0
CA C:CYS47 4.8 25.4 1.0
OH C:TYR95 4.9 34.2 1.0
CD C:GLU70 4.9 27.0 1.0
N C:GLY178 5.0 25.3 1.0
CA C:THR49 5.0 21.8 1.0

Zinc binding site 7 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 7 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn401

b:22.0
occ:1.00
 SG D:CYS113 2.3 19.3 1.0
SG D:CYS105 2.3 20.1 1.0
SG D:CYS99 2.3 20.4 1.0
SG D:CYS102 2.3 19.5 1.0
CB D:CYS113 3.2 18.4 1.0
CB D:CYS102 3.3 23.8 1.0
CB D:CYS105 3.4 22.9 1.0
CB D:CYS99 3.4 20.2 1.0
N D:CYS99 3.6 17.5 1.0
CA D:CYS113 3.6 22.3 1.0
N D:CYS102 3.8 20.8 1.0
N D:GLY114 3.9 27.3 1.0
CA D:CYS99 3.9 19.2 1.0
N D:ARG100 3.9 16.6 1.0
CA D:CYS102 4.1 25.2 1.0
N D:CYS105 4.2 15.2 1.0
C D:CYS113 4.2 23.2 1.0
C D:CYS99 4.3 23.5 1.0
CA D:CYS105 4.4 21.2 1.0
N D:GLU101 4.4 21.8 1.0
N D:LYS115 4.6 20.6 1.0
CB D:LYS115 4.7 24.8 1.0
C D:GLU98 4.7 18.5 1.0
C D:CYS102 4.8 24.5 1.0
CA D:ARG100 4.9 19.8 1.0
C D:GLU101 4.9 32.6 1.0
N D:CYS113 4.9 21.8 1.0
O D:CYS102 5.0 23.2 1.0

Zinc binding site 8 out of 8 in 8co4

Go back to Zinc Binding Sites List in 8co4
Zinc binding site 8 out of 8 in the Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Apo S-Nitrosoglutathione Reductase From Arabidopsis Thalina within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn402

b:34.5
occ:0.95
 NE2 D:HIS69 2.2 29.1 1.0
O D:HOH514 2.2 29.2 1.0
SG D:CYS177 2.3 28.9 1.0
SG D:CYS47 2.3 35.4 1.0
CE1 D:HIS69 3.1 23.2 1.0
CD2 D:HIS69 3.2 27.4 1.0
CB D:CYS47 3.4 21.8 1.0
CB D:CYS177 3.4 31.5 1.0
OG1 D:THR49 3.9 34.8 1.0
OE2 D:GLU70 4.1 33.5 1.0
CB D:THR49 4.1 27.8 1.0
ND1 D:HIS69 4.3 24.0 1.0
CG D:HIS69 4.3 20.6 1.0
CG D:GLU70 4.6 27.5 1.0
NH2 D:ARG372 4.7 25.6 1.0
O D:HOH504 4.7 41.9 1.0
CD D:GLU70 4.8 35.9 1.0
CA D:CYS177 4.8 25.3 1.0
CA D:CYS47 4.8 30.4 1.0
N D:GLY178 4.9 26.1 1.0
N D:THR49 4.9 32.9 1.0

Reference:

M.Meloni, J.Rossi, S.Fanti, G.Carloni, D.Tedesco, P.Treffon, L.Piccinini, G.Falini, P.Trost, E.Vierling, F.Licausi, B.Giuntoli, F.Musiani, S.Fermani, M.Zaffagnini. Structural and Biochemical Characterization of Arabidopsis Alcohol Dehydrogenases Reveals Distinct Functional Properties But Similar Redox Sensitivity. Plant J. 2024.
ISSN: ESSN 1365-313X
PubMed: 38308388
DOI: 10.1111/TPJ.16651
Page generated: Wed Oct 30 18:52:18 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy