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Mercury in PDB 2yaw: Hg Inhibited Sulfur Oxygenase Reductase

Enzymatic activity of Hg Inhibited Sulfur Oxygenase Reductase

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

Protein crystallography data

The structure of Hg Inhibited Sulfur Oxygenase Reductase, PDB code: 2yaw 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) 49.04 / 2.50
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 161.876, 161.876, 154.373, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 18.3

Other elements in 2yaw:

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

Iron (Fe) 6 atoms

Mercury Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Mercury atom in the Hg Inhibited Sulfur Oxygenase Reductase (pdb code 2yaw). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 12 binding sites of Mercury where determined in the Hg Inhibited Sulfur Oxygenase Reductase, PDB code: 2yaw:
Jump to Mercury binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Mercury binding site 1 out of 12 in 2yaw

Go back to Mercury Binding Sites List in 2yaw
Mercury binding site 1 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg404

b:35.7
occ:0.50
 OXT A:ACT405 2.0 15.3 0.5
SG A:CSS31 2.0 34.4 1.0
O A:ACT405 2.7 30.2 0.5
C A:ACT405 2.8 27.3 0.5
CB A:CSS31 3.1 28.9 1.0
O A:GLY27 3.2 28.5 1.0
ND2 A:ASN45 3.3 41.0 1.0
CE2 A:PHE43 3.5 12.8 1.0
C A:GLY27 3.7 27.5 1.0
SD A:CSS31 3.7 0.2 1.0
CZ A:PHE43 3.9 17.2 1.0
CD2 A:PHE43 4.1 15.1 1.0
N A:PRO28 4.2 28.7 1.0
CH3 A:ACT405 4.2 19.1 0.5
CA A:CSS31 4.3 31.4 1.0
CA A:PRO28 4.4 34.5 1.0
N A:CSS31 4.4 25.0 1.0
CA A:GLY27 4.4 23.3 1.0
CG A:ASN45 4.5 41.0 1.0
CE1 A:PHE43 4.8 17.8 1.0
CG A:PHE43 5.0 12.4 1.0
CB A:MET297 5.0 25.4 1.0

Mercury binding site 2 out of 12 in 2yaw

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Mercury binding site 2 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg406

b:65.3
occ:0.30
 SG A:CYS101 2.8 64.3 0.3
O A:CYS101 3.0 57.9 1.0
SD A:MET108 3.7 48.7 1.0
CB A:CYS104 3.8 48.8 1.0
C A:CYS101 3.9 52.7 1.0
CG A:MET108 4.0 43.1 1.0
CE A:MET108 4.0 27.7 1.0
CB A:CYS101 4.2 58.2 1.0
CD A:PRO112 4.3 29.0 1.0
CA A:CYS101 4.5 50.8 1.0
CG A:PRO112 4.5 24.1 1.0
SG A:CYS104 4.6 81.0 1.0
CA A:CYS104 4.9 41.9 1.0
C A:CYS104 4.9 45.0 1.0
CE A:MET210 4.9 7.0 0.3
N A:ALA105 4.9 40.8 1.0
N A:TYR102 4.9 50.9 1.0
SD A:MET210 5.0 51.7 0.3

Mercury binding site 3 out of 12 in 2yaw

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Mercury binding site 3 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg404

b:37.6
occ:0.50
 OXT B:ACT405 1.8 6.7 0.5
SG B:CSS31 2.1 41.5 1.0
C B:ACT405 2.6 29.0 0.5
O B:ACT405 2.6 28.5 0.5
CB B:CSS31 3.0 25.4 1.0
O B:GLY27 3.1 28.3 1.0
ND2 B:ASN45 3.4 44.5 1.0
CE2 B:PHE43 3.6 14.1 1.0
C B:GLY27 3.6 26.8 1.0
SD B:CSS31 3.9 0.8 1.0
CZ B:PHE43 3.9 20.5 1.0
CH3 B:ACT405 4.0 27.4 0.5
N B:PRO28 4.2 28.5 1.0
CD2 B:PHE43 4.2 15.7 1.0
CA B:CSS31 4.2 28.8 1.0
N B:CSS31 4.3 26.8 1.0
CA B:PRO28 4.3 35.1 1.0
CA B:GLY27 4.4 23.3 1.0
CG B:ASN45 4.6 41.7 1.0
CE1 B:PHE43 4.8 23.1 1.0
C B:PRO28 5.0 35.6 1.0
CG B:PHE43 5.0 16.0 1.0

Mercury binding site 4 out of 12 in 2yaw

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Mercury binding site 4 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg406

b:61.4
occ:0.30
 SG B:CYS101 2.6 65.3 0.3
O B:CYS101 2.8 59.0 1.0
CB B:CYS104 3.8 46.2 1.0
C B:CYS101 3.8 51.5 1.0
SD B:MET108 3.9 47.5 1.0
CB B:CYS101 4.1 59.8 1.0
CG B:MET108 4.1 44.3 1.0
CE B:MET108 4.2 28.3 1.0
CA B:CYS101 4.3 51.5 1.0
CD B:PRO112 4.4 27.4 1.0
SG B:CYS104 4.5 82.8 1.0
CG B:PRO112 4.6 19.3 1.0
N B:TYR102 4.8 48.2 1.0
CA B:CYS104 4.8 39.6 1.0
SG B:CYS101 4.9 85.1 0.7
CE B:MET210 4.9 43.3 1.0
C B:CYS104 4.9 45.6 1.0
N B:ALA105 4.9 41.4 1.0

Mercury binding site 5 out of 12 in 2yaw

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Mercury binding site 5 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 5 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Hg404

b:40.4
occ:0.50
 SG C:CSS31 2.0 39.5 1.0
OXT C:ACT405 2.2 7.7 0.5
O C:ACT405 2.5 28.6 0.5
C C:ACT405 2.7 22.3 0.5
CB C:CSS31 3.1 28.2 1.0
O C:GLY27 3.2 29.4 1.0
ND2 C:ASN45 3.4 44.2 1.0
CE2 C:PHE43 3.6 17.1 1.0
C C:GLY27 3.6 27.2 1.0
SD C:CSS31 3.8 80.8 1.0
CZ C:PHE43 4.0 17.2 1.0
N C:PRO28 4.1 31.3 1.0
CD2 C:PHE43 4.2 17.4 1.0
CH3 C:ACT405 4.2 14.2 0.5
CA C:CSS31 4.3 29.4 1.0
CA C:PRO28 4.3 34.0 1.0
CA C:GLY27 4.3 21.9 1.0
N C:CSS31 4.4 20.8 1.0
CG C:ASN45 4.6 41.9 1.0
CE1 C:PHE43 4.8 21.7 1.0
CB C:MET297 5.0 24.0 1.0

Mercury binding site 6 out of 12 in 2yaw

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Mercury binding site 6 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 6 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Hg406

b:60.0
occ:0.30
 SG C:CYS101 2.6 65.4 0.3
O C:CYS101 2.8 57.7 1.0
CB C:CYS104 3.7 47.7 1.0
C C:CYS101 3.7 51.9 1.0
SD C:MET108 3.8 46.5 1.0
CG C:MET108 4.1 42.4 1.0
CB C:CYS101 4.1 59.5 1.0
CE C:MET108 4.2 27.8 1.0
CA C:CYS101 4.3 50.6 1.0
CD C:PRO112 4.4 27.6 1.0
SG C:CYS104 4.4 81.3 1.0
CG C:PRO112 4.7 23.1 1.0
CA C:CYS104 4.7 41.7 1.0
N C:TYR102 4.8 50.5 1.0
C C:CYS104 4.8 45.3 1.0
N C:ALA105 4.8 40.0 1.0
CE C:MET210 4.9 34.9 1.0
SG C:CYS101 4.9 86.3 0.7

Mercury binding site 7 out of 12 in 2yaw

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Mercury binding site 7 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 7 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Hg404

b:36.8
occ:0.50
 SG D:CSS31 2.2 40.0 1.0
O D:ACT405 2.2 20.0 0.5
OXT D:ACT405 2.2 10.8 0.5
C D:ACT405 2.6 24.7 0.5
CB D:CSS31 3.0 25.2 1.0
O D:GLY27 3.1 28.3 1.0
ND2 D:ASN45 3.3 42.9 1.0
CE2 D:PHE43 3.5 13.3 1.0
C D:GLY27 3.6 28.1 1.0
SD D:CSS31 3.9 94.2 1.0
CZ D:PHE43 3.9 18.8 1.0
CH3 D:ACT405 4.1 20.6 0.5
CD2 D:PHE43 4.2 18.8 1.0
N D:PRO28 4.2 31.5 1.0
CA D:CSS31 4.2 21.5 1.0
N D:CSS31 4.3 22.3 1.0
CA D:GLY27 4.3 20.0 1.0
CA D:PRO28 4.3 35.1 1.0
CG D:ASN45 4.5 42.2 1.0
CE1 D:PHE43 4.8 18.6 1.0
CG D:PHE43 5.0 16.0 1.0

Mercury binding site 8 out of 12 in 2yaw

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Mercury binding site 8 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 8 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Hg406

b:65.9
occ:0.30
 SG D:CYS101 2.7 65.1 0.3
O D:CYS101 3.1 58.3 1.0
SD D:MET108 3.7 48.8 1.0
CB D:CYS104 3.9 49.1 1.0
CE D:MET108 4.0 29.1 1.0
C D:CYS101 4.0 52.5 1.0
CG D:MET108 4.0 43.0 1.0
CD D:PRO112 4.1 27.4 1.0
CB D:CYS101 4.2 59.2 1.0
CG D:PRO112 4.4 22.3 1.0
CA D:CYS101 4.5 51.1 1.0
SG D:CYS104 4.6 82.0 1.0
CE D:MET210 4.9 8.4 0.3
SD D:MET210 4.9 47.6 0.3
CB D:PRO112 4.9 20.6 1.0
SG D:CYS101 5.0 85.4 0.7
CA D:CYS104 5.0 41.0 1.0

Mercury binding site 9 out of 12 in 2yaw

Go back to Mercury Binding Sites List in 2yaw
Mercury binding site 9 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 9 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Hg404

b:38.0
occ:0.50
 OXT E:ACT405 1.9 9.0 0.5
SG E:CSS31 2.1 49.0 1.0
O E:ACT405 2.5 29.3 0.5
C E:ACT405 2.6 21.7 0.5
CB E:CSS31 3.1 32.5 1.0
O E:GLY27 3.2 26.2 1.0
ND2 E:ASN45 3.3 42.9 1.0
CE2 E:PHE43 3.6 13.9 1.0
C E:GLY27 3.6 27.6 1.0
SD E:CSS31 3.9 93.5 1.0
CZ E:PHE43 4.0 20.6 1.0
CH3 E:ACT405 4.1 20.8 0.5
N E:PRO28 4.1 31.6 1.0
CD2 E:PHE43 4.2 16.9 1.0
CA E:CSS31 4.3 32.3 1.0
CA E:GLY27 4.3 20.5 1.0
CA E:PRO28 4.3 33.9 1.0
N E:CSS31 4.4 20.7 1.0
CG E:ASN45 4.6 40.9 1.0
CE1 E:PHE43 4.8 19.7 1.0
CB E:MET297 5.0 25.2 1.0

Mercury binding site 10 out of 12 in 2yaw

Go back to Mercury Binding Sites List in 2yaw
Mercury binding site 10 out of 12 in the Hg Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 10 of Hg Inhibited Sulfur Oxygenase Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Hg406

b:73.0
occ:0.30
 SG E:CYS101 2.6 64.6 0.3
O E:CYS101 3.0 59.0 1.0
SD E:MET108 3.8 50.9 1.0
CB E:CYS104 3.8 47.5 1.0
C E:CYS101 3.9 52.1 1.0
CB E:CYS101 4.1 59.6 1.0
CG E:MET108 4.1 43.4 1.0
CE E:MET108 4.1 24.1 1.0
CD E:PRO112 4.3 28.1 1.0
CA E:CYS101 4.4 50.2 1.0
SG E:CYS104 4.4 81.9 1.0
CG E:PRO112 4.5 22.4 1.0
SG E:CYS101 4.8 84.9 0.7
CA E:CYS104 4.9 42.0 1.0
N E:TYR102 4.9 50.6 1.0
C E:CYS104 5.0 44.2 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: Sun Aug 11 03:06:12 2024

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