Iron in PDB 6qjc: Dimethyl Disulfide Inhibited Sulfur Oxygenase Reductase

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

The structure of Dimethyl Disulfide Inhibited Sulfur Oxygenase Reductase, PDB code: 6qjc was solved by C.Frazao, A.Klezin, U.Poell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.20 / 1.70
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	158.400, 158.400, 227.960, 90.00, 90.00, 120.00
R / Rfree (%)	16.5 / 18.8

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

Iron binding site 1 out of 4 in the Dimethyl Disulfide 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 Dimethyl Disulfide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:23.3 occ:0.56 NE2 A:HIS86 2.1 24.9 1.0 NE2 A:HIS90 2.2 40.0 1.0 OE2 A:GLU114 2.3 28.1 1.0 OE1 A:GLU114 2.3 24.4 1.0 O A:HOH656 2.3 40.0 1.0 O A:HOH671 2.4 48.1 1.0 CD A:GLU114 2.6 24.4 1.0 CE1 A:HIS86 2.9 22.8 1.0 CD2 A:HIS90 3.1 41.8 1.0 CE1 A:HIS90 3.2 40.3 1.0 CD2 A:HIS86 3.2 24.8 1.0 ND1 A:HIS86 4.1 26.1 1.0 CG A:GLU114 4.1 18.6 1.0 O A:HOH552 4.2 20.6 1.0 CG A:HIS86 4.2 25.3 1.0 ND1 A:HIS90 4.3 40.9 1.0 CG A:HIS90 4.3 37.0 1.0 CA A:GLY208 4.5 22.1 1.0 OD1 A:ASN9 4.7 40.4 1.0 CE A:MET89 4.8 31.1 1.0 OG1 A:THR78 4.9 24.4 1.0 CB A:ALA7 4.9 21.8 1.0 CB A:GLU114 5.0 20.9 1.0

Iron binding site 2 out of 4 in the Dimethyl Disulfide 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 Dimethyl Disulfide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:20.6 occ:0.60 NE2 B:HIS86 2.1 19.3 1.0 O B:HOH661 2.2 29.2 1.0 OE2 B:GLU114 2.2 22.4 1.0 NE2 B:HIS90 2.2 42.5 1.0 O B:HOH682 2.3 36.7 1.0 OE1 B:GLU114 2.3 24.4 1.0 CD B:GLU114 2.6 22.8 1.0 CE1 B:HIS86 3.0 23.4 1.0 CD2 B:HIS86 3.1 22.7 1.0 CE1 B:HIS90 3.2 41.5 1.0 CD2 B:HIS90 3.2 36.3 1.0 O B:HOH567 4.0 21.6 1.0 CG B:GLU114 4.1 18.1 1.0 ND1 B:HIS86 4.1 23.0 1.0 CG B:HIS86 4.2 21.1 1.0 ND1 B:HIS90 4.3 37.9 1.0 CG B:HIS90 4.4 32.4 1.0 CA B:GLY208 4.6 15.7 1.0 O B:HOH699 4.7 46.8 1.0 CB B:ALA7 4.7 18.7 1.0 OD1 B:ASN9 4.7 47.1 1.0 OG1 B:THR78 4.7 17.4 1.0 CE B:MET89 4.8 30.9 1.0

Iron binding site 3 out of 4 in the Dimethyl Disulfide 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 Dimethyl Disulfide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:24.1 occ:0.56 O C:HOH669 2.1 43.0 1.0 NE2 C:HIS86 2.1 25.1 1.0 OE2 C:GLU114 2.1 27.8 1.0 NE2 C:HIS90 2.2 46.4 1.0 O C:HOH654 2.3 37.5 1.0 OE1 C:GLU114 2.3 29.1 1.0 CD C:GLU114 2.5 28.5 1.0 CE1 C:HIS86 3.0 25.7 1.0 CE1 C:HIS90 3.1 44.3 1.0 CD2 C:HIS86 3.2 23.7 1.0 CD2 C:HIS90 3.2 47.5 1.0 O C:HOH539 4.0 20.3 1.0 CG C:GLU114 4.1 23.5 1.0 ND1 C:HIS86 4.1 25.8 1.0 CG C:HIS86 4.2 23.4 1.0 ND1 C:HIS90 4.3 45.4 1.0 CG C:HIS90 4.3 43.8 1.0 CA C:GLY208 4.7 24.1 1.0 O C:HOH685 4.7 45.1 1.0 CB C:ALA7 4.7 19.5 1.0 OG1 C:THR78 4.7 21.1 1.0 OD1 C:ASN9 4.8 37.7 1.0 CE C:MET89 4.9 38.3 1.0 CB C:GLU114 5.0 20.5 1.0

Iron binding site 4 out of 4 in the Dimethyl Disulfide 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 Dimethyl Disulfide Inhibited Sulfur Oxygenase Reductase within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:19.9 occ:0.60 O D:HOH677 2.0 43.2 1.0 NE2 D:HIS86 2.1 18.3 1.0 O D:HOH679 2.1 29.3 1.0 NE2 D:HIS90 2.2 37.0 1.0 OE2 D:GLU114 2.2 21.6 1.0 OE1 D:GLU114 2.3 24.1 1.0 CD D:GLU114 2.6 21.6 1.0 CE1 D:HIS86 2.9 19.9 1.0 CD2 D:HIS86 3.2 20.2 1.0 CD2 D:HIS90 3.2 32.7 1.0 CE1 D:HIS90 3.2 35.1 1.0 O D:HOH573 4.1 18.9 1.0 CG D:GLU114 4.1 16.2 1.0 ND1 D:HIS86 4.1 19.7 1.0 CG D:HIS86 4.2 20.7 1.0 ND1 D:HIS90 4.3 33.5 1.0 CG D:HIS90 4.3 29.1 1.0 CA D:GLY208 4.6 16.2 1.0 CB D:ALA7 4.7 17.8 1.0 OD1 D:ASN9 4.7 41.5 1.0 CE D:MET89 4.8 33.1 1.0 OG1 D:THR78 4.8 15.4 1.0 O D:HOH712 4.9 39.0 1.0 CB D:GLU114 5.0 14.6 1.0

C.Frazao, A.Klezin. Multiple Sulfane Modifications in Active-Site Cysteine Thiols of Two Sulfur Oxygenase Reductases and Analysis of Substrate/Product Channels To Be Published.