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Chlorine in PDB 2yav: Zn Inhibited Sulfur Oxygenase Reductase

Enzymatic activity of Zn Inhibited Sulfur Oxygenase Reductase

All present enzymatic activity of Zn Inhibited Sulfur Oxygenase Reductase:
1.13.11.55;

Protein crystallography data

The structure of Zn Inhibited Sulfur Oxygenase Reductase, PDB code: 2yav was solved by A.Veith, T.Urich, K.Seyfarth, J.Protze, C.Frazao, A.Kletzin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.20 / 1.70
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 162.074, 162.074, 154.237, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 19.3

Other elements in 2yav:

The structure of Zn Inhibited Sulfur Oxygenase Reductase also contains other interesting chemical elements:

Zinc (Zn) 6 atoms
Iron (Fe) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Zn Inhibited Sulfur Oxygenase Reductase (pdb code 2yav). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Zn Inhibited Sulfur Oxygenase Reductase, PDB code: 2yav:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 2yav

Go back to Chlorine Binding Sites List in 2yav
Chlorine binding site 1 out of 6 in the Zn Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Zn Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl407

b:20.9
occ:0.80
 ZN A:ZN405 2.3 23.5 0.8
O A:HOH2198 3.2 44.8 1.0
CG A:PRO288 3.4 19.2 1.0
OXT A:ACT406 3.4 28.3 0.8
NE2 A:HIS277 3.6 14.2 1.0
O A:HOH2233 3.6 19.2 0.8
CB A:PRO288 3.6 21.0 1.0
CE1 A:HIS277 3.7 13.0 1.0
O A:HOH2232 3.9 26.0 0.8
CZ A:PHE54 3.9 21.0 1.0
CE1 A:PHE54 4.1 20.0 1.0
CD1 A:ILE290 4.1 14.9 1.0
C A:ACT406 4.4 24.6 0.8
CG2 A:VAL267 4.5 14.4 1.0
O A:ACT406 4.5 23.0 0.8
CD A:PRO288 4.7 17.0 1.0
CD2 A:HIS277 4.8 17.8 1.0
ND1 A:HIS277 4.9 14.8 1.0

Chlorine binding site 2 out of 6 in 2yav

Go back to Chlorine Binding Sites List in 2yav
Chlorine binding site 2 out of 6 in the Zn Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Zn Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl407

b:21.1
occ:0.80
 ZN B:ZN405 2.2 24.2 0.8
CG B:PRO288 3.4 20.1 1.0
O B:HOH2222 3.5 26.9 0.8
NE2 B:HIS277 3.5 16.7 1.0
O B:HOH2221 3.6 24.0 0.8
OXT B:ACT406 3.6 26.3 0.8
CB B:PRO288 3.6 20.4 1.0
CE1 B:HIS277 3.7 18.3 1.0
CZ B:PHE54 4.0 17.4 1.0
CE1 B:PHE54 4.1 21.5 1.0
CD1 B:ILE290 4.1 16.6 1.0
CG2 B:VAL267 4.5 15.6 1.0
C B:ACT406 4.5 27.9 0.8
CD B:PRO288 4.7 16.9 1.0
O B:ACT406 4.7 26.3 0.8
CD2 B:HIS277 4.8 15.4 1.0
ND1 B:HIS277 4.9 15.2 1.0

Chlorine binding site 3 out of 6 in 2yav

Go back to Chlorine Binding Sites List in 2yav
Chlorine binding site 3 out of 6 in the Zn Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Zn Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl407

b:20.9
occ:0.80
 ZN C:ZN405 2.2 22.1 0.8
O C:HOH2189 2.7 41.8 1.0
CG C:PRO288 3.5 17.6 1.0
O C:HOH2221 3.5 19.0 0.8
OXT C:ACT406 3.5 28.2 0.8
NE2 C:HIS277 3.6 18.1 1.0
CB C:PRO288 3.6 21.2 1.0
O C:HOH2220 3.7 28.5 0.8
CE1 C:HIS277 3.7 16.5 1.0
CZ C:PHE54 4.0 20.0 1.0
CD1 C:ILE290 4.1 16.0 1.0
CE1 C:PHE54 4.1 16.5 1.0
C C:ACT406 4.4 21.2 0.8
CG2 C:VAL267 4.5 12.0 1.0
O C:ACT406 4.6 22.4 0.8
CD2 C:HIS277 4.8 16.2 1.0
CD C:PRO288 4.8 17.2 1.0
ND1 C:HIS277 4.9 16.9 1.0

Chlorine binding site 4 out of 6 in 2yav

Go back to Chlorine Binding Sites List in 2yav
Chlorine binding site 4 out of 6 in the Zn Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Zn Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl407

b:23.5
occ:0.80
 ZN D:ZN405 2.2 24.2 0.8
O D:HOH2193 3.0 35.8 1.0
CG D:PRO288 3.4 23.1 1.0
OXT D:ACT406 3.4 26.7 0.8
NE2 D:HIS277 3.6 16.6 1.0
CB D:PRO288 3.6 18.4 1.0
O D:HOH2225 3.7 25.0 0.8
CE1 D:HIS277 3.7 15.9 1.0
O D:HOH2226 3.8 29.9 0.8
CZ D:PHE54 3.9 18.7 1.0
CE1 D:PHE54 4.1 21.0 1.0
CD1 D:ILE290 4.1 17.6 1.0
C D:ACT406 4.3 24.5 0.8
O D:ACT406 4.5 24.6 0.8
CG2 D:VAL267 4.5 12.8 1.0
CD D:PRO288 4.7 15.6 1.0
CD2 D:HIS277 4.8 17.1 1.0
ND1 D:HIS277 4.9 14.8 1.0

Chlorine binding site 5 out of 6 in 2yav

Go back to Chlorine Binding Sites List in 2yav
Chlorine binding site 5 out of 6 in the Zn Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Zn Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cl407

b:21.5
occ:0.80
 ZN E:ZN405 2.2 24.3 0.8
O E:HOH2183 3.1 43.4 1.0
OXT E:ACT406 3.4 30.9 0.8
CG E:PRO288 3.4 17.5 1.0
O E:HOH2215 3.5 36.4 0.8
NE2 E:HIS277 3.5 18.8 1.0
CE1 E:HIS277 3.6 14.7 1.0
O E:HOH2214 3.7 19.0 0.8
CB E:PRO288 3.7 22.1 1.0
CZ E:PHE54 4.0 19.9 1.0
CE1 E:PHE54 4.1 20.1 1.0
CD1 E:ILE290 4.2 14.9 1.0
C E:ACT406 4.4 26.7 0.8
CG2 E:VAL267 4.4 13.2 1.0
O E:ACT406 4.6 25.8 0.8
CD E:PRO288 4.7 18.1 1.0
CD2 E:HIS277 4.8 16.4 1.0
ND1 E:HIS277 4.8 12.0 1.0

Chlorine binding site 6 out of 6 in 2yav

Go back to Chlorine Binding Sites List in 2yav
Chlorine binding site 6 out of 6 in the Zn Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Zn Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl407

b:21.7
occ:0.80
 ZN F:ZN405 2.2 24.0 0.8
CG F:PRO288 3.3 21.8 1.0
OXT F:ACT406 3.5 28.9 0.8
CB F:PRO288 3.6 18.8 1.0
NE2 F:HIS277 3.6 16.8 1.0
O F:HOH2240 3.7 24.2 0.8
CE1 F:HIS277 3.7 13.7 1.0
O F:HOH2241 3.8 28.2 0.8
CZ F:PHE54 3.9 16.9 1.0
CE1 F:PHE54 4.0 16.1 1.0
CD1 F:ILE290 4.1 16.2 1.0
C F:ACT406 4.4 20.9 0.8
CG2 F:VAL267 4.6 16.2 1.0
O F:ACT406 4.7 25.1 0.8
CD F:PRO288 4.7 17.3 1.0
CD2 F:HIS277 4.9 17.9 1.0
ND1 F:HIS277 4.9 14.6 1.0
CG1 F:ILE290 5.0 16.0 1.0

Reference:

A.Veith, T.Urich, K.Seyfarth, J.Protze, C.Frazao, A.Kletzin. Substrate Pathways and Mechanisms of Inhibition in the Sulfur Oxygenase Reductase of Acidianus Ambivalens. Front.Microbiol. V. 2 37 2011.
ISSN: ESSN 1664-302X
PubMed: 21747782
DOI: 10.3389/FMICB.2011.00037
Page generated: Sat Jul 20 14:54:22 2024

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