Iron in PDB 2yax: Iodoacetamide Inhibited Sulfur Oxygenase Reductase

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

The structure of Iodoacetamide Inhibited Sulfur Oxygenase Reductase, PDB code: 2yax 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)	38.05 / 1.80
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	161.897, 161.897, 154.273, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 19.3

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

Iron binding site 1 out of 6 in the Iodoacetamide Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Iodoacetamide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1309 b:34.5 occ:1.00 NE2 A:HIS86 2.1 28.1 1.0 O A:HOH2018 2.2 35.0 1.0 NE2 A:HIS90 2.2 39.6 1.0 OE2 A:GLU114 2.2 28.8 1.0 O A:HOH2015 2.2 36.5 1.0 OE1 A:GLU114 2.3 28.2 1.0 CD A:GLU114 2.5 26.3 1.0 CE1 A:HIS86 3.1 30.5 1.0 CE1 A:HIS90 3.1 39.3 1.0 CD2 A:HIS86 3.1 26.9 1.0 CD2 A:HIS90 3.2 38.0 1.0 O A:HOH2022 4.0 31.5 1.0 CG A:GLU114 4.1 24.5 1.0 ND1 A:HIS86 4.2 29.2 1.0 CG A:HIS86 4.3 26.3 1.0 ND1 A:HIS90 4.3 39.0 1.0 CG A:HIS90 4.3 33.1 1.0 CA A:GLY208 4.7 27.0 1.0 OG1 A:THR78 4.7 22.9 1.0 CB A:ALA7 4.7 21.3 1.0 CE A:MET89 4.8 36.9 1.0 CB A:GLU114 5.0 25.0 1.0

Iron binding site 2 out of 6 in the Iodoacetamide Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Iodoacetamide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1309 b:33.4 occ:1.00 O B:HOH2023 2.1 30.8 1.0 NE2 B:HIS86 2.2 26.5 1.0 OE2 B:GLU114 2.2 30.5 1.0 NE2 B:HIS90 2.2 39.0 1.0 O B:HOH2020 2.2 34.6 1.0 OE1 B:GLU114 2.3 28.2 1.0 CD B:GLU114 2.5 26.8 1.0 CE1 B:HIS86 3.1 29.4 1.0 CD2 B:HIS86 3.1 25.9 1.0 CE1 B:HIS90 3.2 36.7 1.0 CD2 B:HIS90 3.2 35.9 1.0 O B:HOH2027 4.0 26.8 1.0 CG B:GLU114 4.0 26.6 1.0 ND1 B:HIS86 4.2 27.4 1.0 CG B:HIS86 4.3 27.3 1.0 ND1 B:HIS90 4.3 38.5 1.0 CG B:HIS90 4.3 31.9 1.0 CB B:ALA7 4.7 23.4 1.0 CA B:GLY208 4.7 25.7 1.0 OG1 B:THR78 4.7 26.9 1.0 CE B:MET89 4.8 39.5 1.0 CB B:GLU114 5.0 25.9 1.0

Iron binding site 3 out of 6 in the Iodoacetamide Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Iodoacetamide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1309 b:34.9 occ:1.00 NE2 C:HIS86 2.2 30.7 1.0 OE2 C:GLU114 2.2 31.2 1.0 O C:HOH2024 2.2 36.1 1.0 NE2 C:HIS90 2.2 38.3 1.0 O C:HOH2017 2.2 32.9 1.0 OE1 C:GLU114 2.3 27.0 1.0 CD C:GLU114 2.5 29.4 1.0 CE1 C:HIS86 3.1 28.0 1.0 CE1 C:HIS90 3.1 37.8 1.0 CD2 C:HIS86 3.2 27.3 1.0 CD2 C:HIS90 3.2 35.4 1.0 CG C:GLU114 4.0 25.8 1.0 O C:HOH2016 4.1 27.6 1.0 ND1 C:HIS86 4.2 30.3 1.0 ND1 C:HIS90 4.3 39.6 1.0 CG C:HIS86 4.3 28.2 1.0 CG C:HIS90 4.3 33.5 1.0 CA C:GLY208 4.7 29.5 1.0 OG1 C:THR78 4.7 28.5 1.0 CB C:ALA7 4.7 25.4 1.0 CE C:MET89 4.8 42.5 1.0 CB C:GLU114 4.9 26.3 1.0

Iron binding site 4 out of 6 in the Iodoacetamide Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Iodoacetamide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1309 b:34.6 occ:1.00 NE2 D:HIS86 2.1 28.9 1.0 O D:HOH2024 2.2 32.2 1.0 O D:HOH2020 2.2 35.6 1.0 NE2 D:HIS90 2.2 39.7 1.0 OE2 D:GLU114 2.2 26.9 1.0 OE1 D:GLU114 2.3 28.7 1.0 CD D:GLU114 2.6 28.8 1.0 CE1 D:HIS86 3.1 27.1 1.0 CD2 D:HIS86 3.1 25.7 1.0 CE1 D:HIS90 3.1 38.8 1.0 CD2 D:HIS90 3.2 38.4 1.0 O D:HOH2028 4.0 28.6 1.0 CG D:GLU114 4.1 28.3 1.0 ND1 D:HIS86 4.2 28.4 1.0 CG D:HIS86 4.2 28.1 1.0 ND1 D:HIS90 4.3 39.2 1.0 CG D:HIS90 4.3 30.3 1.0 CA D:GLY208 4.7 27.7 1.0 OG1 D:THR78 4.7 25.3 1.0 CB D:ALA7 4.7 26.1 1.0 CE D:MET89 4.8 37.1 1.0 CB D:GLU114 5.0 24.7 1.0

Iron binding site 5 out of 6 in the Iodoacetamide Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Iodoacetamide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe1309 b:33.5 occ:1.00 O E:HOH2023 2.1 35.2 1.0 NE2 E:HIS86 2.1 27.6 1.0 NE2 E:HIS90 2.2 35.7 1.0 OE2 E:GLU114 2.2 27.5 1.0 O E:HOH2018 2.2 33.8 1.0 OE1 E:GLU114 2.3 28.1 1.0 CD E:GLU114 2.5 27.9 1.0 CE1 E:HIS86 3.1 27.6 1.0 CE1 E:HIS90 3.1 39.9 1.0 CD2 E:HIS86 3.1 26.5 1.0 CD2 E:HIS90 3.2 34.9 1.0 CG E:GLU114 4.1 23.0 1.0 O E:HOH2024 4.1 28.2 1.0 ND1 E:HIS86 4.2 28.9 1.0 ND1 E:HIS90 4.3 34.9 1.0 CG E:HIS86 4.3 27.1 1.0 CG E:HIS90 4.3 30.5 1.0 CA E:GLY208 4.6 30.2 1.0 CB E:ALA7 4.7 25.5 1.0 OG1 E:THR78 4.7 24.6 1.0 CE E:MET89 4.8 39.2 1.0 CB E:GLU114 4.9 26.1 1.0

Iron binding site 6 out of 6 in the Iodoacetamide Inhibited Sulfur Oxygenase Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Iodoacetamide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe1309 b:32.1 occ:1.00 NE2 F:HIS86 2.1 28.5 1.0 NE2 F:HIS90 2.2 38.8 1.0 OE2 F:GLU114 2.2 28.6 1.0 OE1 F:GLU114 2.2 27.8 1.0 O F:HOH2025 2.2 32.5 1.0 O F:HOH2015 2.3 33.3 1.0 CD F:GLU114 2.5 24.8 1.0 CE1 F:HIS86 3.0 28.9 1.0 CE1 F:HIS90 3.1 38.7 1.0 CD2 F:HIS86 3.2 25.4 1.0 CD2 F:HIS90 3.2 35.9 1.0 O F:HOH2024 4.0 26.2 1.0 CG F:GLU114 4.0 25.1 1.0 ND1 F:HIS86 4.1 29.6 1.0 ND1 F:HIS90 4.2 37.1 1.0 CG F:HIS86 4.3 26.7 1.0 CG F:HIS90 4.3 36.2 1.0 CA F:GLY208 4.6 29.5 1.0 CB F:ALA7 4.8 22.9 1.0 OG1 F:THR78 4.8 24.2 1.0 CE F:MET89 4.8 38.4 1.0 CB F:GLU114 4.9 27.3 1.0

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