Iron in PDB 6e0y: A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH

The structure of A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH, PDB code: 6e0y was solved by M.Smith, K.Lancaster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.19 / 2.26
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.031, 80.941, 120.598, 90.00, 96.03, 90.00
R / Rfree (%)	19.3 / 24.2

The binding sites of Iron atom in the A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH (pdb code 6e0y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH, PDB code: 6e0y:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:46.0 occ:1.00 FE A:HEC201 0.0 46.0 1.0 NA A:HEC201 2.0 47.0 1.0 NB A:HEC201 2.1 49.5 1.0 NC A:HEC201 2.1 51.7 1.0 ND A:HEC201 2.1 51.3 1.0 NE2 A:HIS172 2.4 41.8 1.0 N A:HOA202 2.7 52.8 1.0 C4A A:HEC201 3.0 48.2 1.0 C1A A:HEC201 3.0 48.0 1.0 C1B A:HEC201 3.0 46.4 1.0 C4C A:HEC201 3.1 49.8 1.0 C4B A:HEC201 3.1 50.2 1.0 C1C A:HEC201 3.1 52.0 1.0 C1D A:HEC201 3.1 47.7 1.0 C4D A:HEC201 3.1 49.5 1.0 CE1 A:HIS172 3.3 45.4 1.0 CHB A:HEC201 3.4 44.3 1.0 CD2 A:HIS172 3.4 47.4 1.0 CHA A:HEC201 3.4 47.6 1.0 CHD A:HEC201 3.4 49.2 1.0 CHC A:HEC201 3.5 51.0 1.0 O A:HOA202 3.6 58.8 1.0 C3A A:HEC201 4.2 42.4 1.0 C2A A:HEC201 4.2 42.2 1.0 C2B A:HEC201 4.3 49.3 1.0 C3B A:HEC201 4.3 47.8 1.0 C3C A:HEC201 4.3 52.5 1.0 C2C A:HEC201 4.3 50.3 1.0 C2D A:HEC201 4.4 48.5 1.0 C3D A:HEC201 4.4 43.5 1.0 ND1 A:HIS172 4.4 49.6 1.0 CG A:HIS172 4.5 51.7 1.0 OE1 A:GLN131 4.6 53.1 1.0 NZ A:LYS106 4.7 45.7 1.0 CE2 A:PHE182 4.9 48.4 1.0

Iron binding site 2 out of 4 in the A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:40.8 occ:1.00 FE B:HEC201 0.0 40.8 1.0 ND B:HEC201 2.0 37.3 1.0 NB B:HEC201 2.0 36.4 1.0 NA B:HEC201 2.1 43.9 1.0 NC B:HEC201 2.1 40.1 1.0 NE2 B:HIS172 2.4 42.3 1.0 N B:HOA202 2.7 45.5 1.0 C1D B:HEC201 3.0 38.6 1.0 C1A B:HEC201 3.0 45.0 1.0 C1B B:HEC201 3.0 41.2 1.0 C4A B:HEC201 3.0 40.5 1.0 C4D B:HEC201 3.0 40.8 1.0 C4C B:HEC201 3.1 39.0 1.0 C4B B:HEC201 3.1 41.8 1.0 C1C B:HEC201 3.2 35.8 1.0 CD2 B:HIS172 3.3 39.5 1.0 CHD B:HEC201 3.4 40.1 1.0 CHB B:HEC201 3.4 41.7 1.0 CHA B:HEC201 3.4 44.1 1.0 CE1 B:HIS172 3.4 42.6 1.0 CHC B:HEC201 3.5 40.7 1.0 O B:HOA202 3.9 46.5 1.0 C3A B:HEC201 4.2 39.1 1.0 C2A B:HEC201 4.2 43.8 1.0 C2D B:HEC201 4.3 40.8 1.0 C2B B:HEC201 4.3 42.5 1.0 C3D B:HEC201 4.3 39.5 1.0 C3B B:HEC201 4.3 42.8 1.0 C3C B:HEC201 4.3 35.3 1.0 C2C B:HEC201 4.4 41.1 1.0 CG B:HIS172 4.5 48.7 1.0 ND1 B:HIS172 4.5 46.5 1.0 NZ B:LYS106 4.5 44.0 1.0 NE2 B:GLN131 4.9 44.6 1.0 CE2 B:PHE182 5.0 43.4 1.0

Iron binding site 3 out of 4 in the A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:47.2 occ:1.00 FE C:HEC201 0.0 47.2 1.0 NC C:HEC201 2.0 44.3 1.0 NB C:HEC201 2.0 47.4 1.0 NA C:HEC201 2.1 47.4 1.0 ND C:HEC201 2.1 44.4 1.0 NE2 C:HIS172 2.4 47.0 1.0 N C:HOA202 2.7 48.4 1.0 C1B C:HEC201 3.0 49.9 1.0 C4A C:HEC201 3.0 42.5 1.0 C4C C:HEC201 3.0 46.6 1.0 C1A C:HEC201 3.1 46.5 1.0 C1D C:HEC201 3.1 46.7 1.0 C1C C:HEC201 3.1 42.1 1.0 C4B C:HEC201 3.1 53.5 1.0 C4D C:HEC201 3.2 45.4 1.0 CE1 C:HIS172 3.3 47.3 1.0 CHB C:HEC201 3.4 47.9 1.0 CHD C:HEC201 3.4 45.2 1.0 CD2 C:HIS172 3.4 47.0 1.0 CHA C:HEC201 3.5 45.2 1.0 CHC C:HEC201 3.5 49.3 1.0 O C:HOA202 3.9 52.1 1.0 C3A C:HEC201 4.2 46.9 1.0 C2A C:HEC201 4.2 48.0 1.0 C2B C:HEC201 4.2 50.2 1.0 C3C C:HEC201 4.3 44.9 1.0 C2C C:HEC201 4.3 46.7 1.0 C3B C:HEC201 4.3 52.8 1.0 C2D C:HEC201 4.3 45.6 1.0 C3D C:HEC201 4.4 43.1 1.0 ND1 C:HIS172 4.4 47.1 1.0 CG C:HIS172 4.5 45.1 1.0 NZ C:LYS106 4.5 45.3 1.0 OE1 C:GLN131 4.6 49.5 1.0 CE2 C:PHE182 4.9 46.7 1.0

Iron binding site 4 out of 4 in the A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of A131Q Mutant of Cyt P460 of Nitrosomonas Sp. AL212 with Bound NH2OH within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:50.5 occ:1.00 FE D:HEC201 0.0 50.5 1.0 NB D:HEC201 2.0 52.3 1.0 NA D:HEC201 2.1 55.2 1.0 ND D:HEC201 2.1 54.9 1.0 NC D:HEC201 2.1 57.6 1.0 NE2 D:HIS172 2.4 46.5 1.0 N D:HOA202 2.7 57.9 1.0 C4A D:HEC201 3.0 49.1 1.0 C1B D:HEC201 3.0 53.4 1.0 C1A D:HEC201 3.0 52.2 1.0 C1D D:HEC201 3.1 51.0 1.0 C4C D:HEC201 3.1 54.0 1.0 C4D D:HEC201 3.1 53.4 1.0 C4B D:HEC201 3.1 56.3 1.0 C1C D:HEC201 3.1 55.9 1.0 CD2 D:HIS172 3.3 48.8 1.0 CE1 D:HIS172 3.3 51.4 1.0 CHB D:HEC201 3.3 50.6 1.0 CHD D:HEC201 3.4 52.3 1.0 CHA D:HEC201 3.4 50.6 1.0 CHC D:HEC201 3.5 53.6 1.0 O D:HOA202 3.9 62.5 1.0 C3A D:HEC201 4.1 44.0 1.0 C2A D:HEC201 4.1 45.9 1.0 C2B D:HEC201 4.3 53.8 1.0 C2D D:HEC201 4.3 53.0 1.0 C3B D:HEC201 4.3 51.5 1.0 C3C D:HEC201 4.3 55.3 1.0 C3D D:HEC201 4.3 47.1 1.0 C2C D:HEC201 4.4 57.7 1.0 ND1 D:HIS172 4.4 53.4 1.0 CG D:HIS172 4.5 54.1 1.0 NZ D:LYS106 4.6 48.8 1.0 NE2 D:GLN131 4.6 57.3 1.0 CE2 D:PHE182 4.9 53.2 1.0

M.A.Smith, S.H.Majer, A.C.Vilbert, K.M.Lancaster. Controlling A Burn: Outer-Sphere Gating of Hydroxylamine Oxidation By A Distal Base in Cytochrome P460. Chem Sci V. 10 3756 2019.
ISSN: ISSN 2041-6520
PubMed: 31015919
DOI: 10.1039/C9SC00195F