Iron in PDB 6qo0: I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens

All present enzymatic activity of I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens:
1.13.11.55;

The structure of I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens, PDB code: 6qo0 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)	113.80 / 1.65
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	158.160, 158.160, 227.640, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 19.1

The binding sites of Iron atom in the I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens (pdb code 6qo0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens, PDB code: 6qo0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:28.6 occ:0.44 NE2 A:HIS86 2.1 27.9 1.0 O A:HOH635 2.1 44.8 1.0 O A:HOH663 2.2 44.4 1.0 OE2 A:GLU114 2.2 32.1 1.0 NE2 A:HIS90 2.3 42.0 1.0 OE1 A:GLU114 2.3 32.2 1.0 CD A:GLU114 2.6 33.9 1.0 CE1 A:HIS86 3.0 28.2 1.0 CD2 A:HIS86 3.1 30.0 1.0 CD2 A:HIS90 3.2 43.4 1.0 CE1 A:HIS90 3.3 43.6 1.0 O A:HOH564 4.1 29.4 1.0 CG A:GLU114 4.1 25.2 1.0 ND1 A:HIS86 4.2 29.2 1.0 CG A:HIS86 4.2 29.3 1.0 CG A:HIS90 4.4 39.2 1.0 ND1 A:HIS90 4.4 43.0 1.0 O A:HOH705 4.5 54.1 1.0 CA A:GLY208 4.6 26.9 1.0 OG1 A:THR78 4.8 29.4 1.0 CB A:ALA7 4.8 28.8 1.0 CE A:MET89 4.8 37.3 1.0 CB A:GLU114 5.0 27.5 1.0

Iron binding site 2 out of 4 in the I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:25.2 occ:0.46 NE2 B:HIS86 2.1 25.4 1.0 O B:HOH670 2.1 32.9 1.0 O B:HOH663 2.2 36.1 1.0 OE2 B:GLU114 2.2 29.3 1.0 NE2 B:HIS90 2.2 39.2 1.0 OE1 B:GLU114 2.3 31.3 1.0 CD B:GLU114 2.6 28.3 1.0 CE1 B:HIS86 3.0 26.4 1.0 CD2 B:HIS86 3.1 27.2 1.0 CE1 B:HIS90 3.2 36.0 1.0 CD2 B:HIS90 3.2 35.2 1.0 O B:HOH550 4.0 27.3 1.0 CG B:GLU114 4.1 21.6 1.0 ND1 B:HIS86 4.1 27.2 1.0 CG B:HIS86 4.2 27.6 1.0 ND1 B:HIS90 4.3 36.0 1.0 CG B:HIS90 4.4 33.8 1.0 O B:HOH505 4.4 50.0 1.0 CA B:GLY208 4.6 21.2 1.0 CB B:ALA7 4.7 21.5 1.0 OG1 B:THR78 4.8 24.4 1.0 CE B:MET89 4.9 36.1 1.0 O B:HOH713 4.9 45.3 1.0 CB B:GLU114 5.0 22.7 1.0

Iron binding site 3 out of 4 in the I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:32.4 occ:0.49 O C:HOH682 2.1 42.9 1.0 OE2 C:GLU114 2.2 32.7 1.0 NE2 C:HIS86 2.2 31.5 1.0 O C:HOH664 2.2 44.8 1.0 NE2 C:HIS90 2.2 47.8 1.0 OE1 C:GLU114 2.3 32.2 1.0 CD C:GLU114 2.6 30.8 1.0 CE1 C:HIS86 3.1 31.7 1.0 CE1 C:HIS90 3.1 46.6 1.0 CD2 C:HIS86 3.2 30.7 1.0 CD2 C:HIS90 3.2 48.1 1.0 O C:HOH559 3.9 26.9 1.0 CG C:GLU114 4.1 27.3 1.0 ND1 C:HIS86 4.2 30.1 1.0 ND1 C:HIS90 4.3 47.9 1.0 CG C:HIS86 4.3 28.6 1.0 CG C:HIS90 4.3 45.0 1.0 CA C:GLY208 4.6 27.7 1.0 OG1 C:THR78 4.7 28.0 1.0 CB C:ALA7 4.8 24.7 1.0 O C:HOH708 4.9 51.5 1.0 CE C:MET89 4.9 39.5 1.0

Iron binding site 4 out of 4 in the I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of I47W Mutated Sulfur Oxygenase Reductase From Acidianus Ambivaens within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:25.7 occ:0.44 O D:HOH666 2.1 39.4 1.0 NE2 D:HIS86 2.1 26.8 1.0 O D:HOH658 2.2 35.6 1.0 OE2 D:GLU114 2.2 28.6 1.0 NE2 D:HIS90 2.2 39.3 1.0 OE1 D:GLU114 2.2 30.8 1.0 CD D:GLU114 2.5 27.9 1.0 CE1 D:HIS86 3.0 26.0 1.0 CE1 D:HIS90 3.2 37.8 1.0 CD2 D:HIS86 3.2 27.8 1.0 CD2 D:HIS90 3.2 37.4 1.0 CG D:GLU114 4.0 24.7 1.0 O D:HOH564 4.0 27.0 1.0 ND1 D:HIS86 4.1 26.6 1.0 CG D:HIS86 4.2 28.4 1.0 ND1 D:HIS90 4.3 39.0 1.0 CG D:HIS90 4.3 31.2 1.0 CA D:GLY208 4.6 24.2 1.0 CB D:ALA7 4.7 21.2 1.0 OG1 D:THR78 4.8 22.9 1.0 O D:HOH723 4.9 42.4 1.0 CB D:GLU114 4.9 22.6 1.0 CE D:MET89 5.0 37.4 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.