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Chlorine in PDB 7z3f: Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form

Protein crystallography data

The structure of Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form, PDB code: 7z3f was solved by P.Leone, G.Sciara, M.Ilbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.26 / 1.70
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.477, 73.477, 112.902, 90, 90, 90
R / Rfree (%) 23.6 / 26

Other elements in 7z3f:

The structure of Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form also contains other interesting chemical elements:

Sodium (Na) 2 atoms
Copper (Cu) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form (pdb code 7z3f). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form, PDB code: 7z3f:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7z3f

Go back to Chlorine Binding Sites List in 7z3f
Chlorine binding site 1 out of 2 in the Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl205

b:40.7
occ:1.00
O A:CYS159 2.6 19.7 1.0
O A:LEU161 2.7 27.6 1.0
CA A:GLY164 2.9 27.4 1.0
N A:PHE167 3.0 20.2 1.0
C A:GLY164 3.0 26.1 1.0
C A:PHE160 3.1 23.5 1.0
N A:HIS166 3.2 20.8 1.0
CA A:PHE160 3.3 21.4 1.0
N A:LEU161 3.3 23.1 1.0
O A:GLY164 3.4 27.1 1.0
C A:CYS159 3.4 19.8 1.0
N A:GLY164 3.5 27.5 1.0
N A:GLN165 3.5 25.7 1.0
CB A:HIS166 3.5 20.4 1.0
O A:PHE160 3.5 22.1 1.0
CB A:PHE167 3.6 21.7 1.0
CA A:HIS166 3.6 20.6 1.0
N A:PHE160 3.7 20.2 1.0
C A:HIS166 3.8 20.6 1.0
C A:LEU161 3.8 27.6 1.0
CA A:PHE167 3.9 21.2 1.0
C A:GLN165 4.0 24.1 1.0
CA A:LEU161 4.2 25.0 1.0
CG A:HIS166 4.2 21.4 1.0
CA A:GLN165 4.4 26.8 1.0
SG A:CYS159 4.6 21.6 1.0
CB A:PHE160 4.7 21.3 1.0
CD2 A:HIS166 4.7 24.2 1.0
CA A:CYS159 4.7 19.3 1.0
CB A:CYS159 4.7 18.3 1.0
C A:THR163 4.8 30.4 1.0
O A:GLN165 4.9 23.2 1.0
CG A:PHE167 5.0 22.8 1.0
O A:HIS166 5.0 21.3 1.0

Chlorine binding site 2 out of 2 in 7z3f

Go back to Chlorine Binding Sites List in 7z3f
Chlorine binding site 2 out of 2 in the Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans, Oxidized Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl205

b:50.2
occ:1.00
O B:LEU161 2.6 41.0 1.0
O B:CYS159 2.8 27.0 1.0
C B:GLY164 2.8 41.6 1.0
CA B:GLY164 2.9 41.6 1.0
N B:HIS166 3.0 34.5 1.0
N B:PHE167 3.0 31.3 1.0
C B:PHE160 3.2 35.4 1.0
N B:GLN165 3.2 38.6 1.0
O B:GLY164 3.3 45.3 1.0
CA B:PHE160 3.3 34.3 1.0
N B:GLY164 3.4 44.3 1.0
N B:LEU161 3.4 35.7 1.0
CB B:HIS166 3.5 30.7 1.0
CA B:HIS166 3.5 31.6 1.0
C B:CYS159 3.5 28.4 1.0
O B:PHE160 3.5 38.0 1.0
C B:LEU161 3.7 40.7 1.0
C B:HIS166 3.7 32.0 1.0
C B:GLN165 3.8 35.5 1.0
N B:PHE160 3.8 29.5 1.0
CB B:PHE167 3.8 33.7 1.0
CA B:PHE167 4.0 32.5 1.0
CA B:GLN165 4.1 39.1 1.0
CA B:LEU161 4.2 37.8 1.0
CG B:HIS166 4.2 30.3 1.0
CD2 B:HIS166 4.6 31.8 1.0
C B:THR163 4.6 50.0 1.0
CB B:PHE160 4.7 35.7 1.0
O B:GLN165 4.7 35.3 1.0
SG B:CYS159 4.7 26.1 1.0
O B:GLN162 4.9 43.3 1.0
CA B:CYS159 4.9 26.3 1.0
N B:GLN162 4.9 43.4 1.0
C B:GLN162 5.0 46.1 1.0
O B:HIS166 5.0 32.5 1.0

Reference:

P.Leone, G.Sciara, M.Ilbert. Crystal Structure of the Cupredoxin Acop From Acidithiobacillus Ferrooxidans To Be Published.
Page generated: Thu Dec 28 02:59:24 2023

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