Iron in PDB 6w6n: K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212

The structure of K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212, PDB code: 6w6n was solved by R.E.Coleman, K.M.Lancaster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.38 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.373, 80.172, 110.767, 90.00, 90.00, 90.00
R / Rfree (%)	25.8 / 27.8

The binding sites of Iron atom in the K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212 (pdb code 6w6n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212, PDB code: 6w6n:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:48.1 occ:1.00 FE A:HEC201 0.0 48.1 1.0 NC A:HEC201 2.0 56.8 1.0 NA A:HEC201 2.1 52.2 1.0 ND A:HEC201 2.1 54.8 1.0 NB A:HEC201 2.1 53.6 1.0 NE2 A:HIS172 2.1 29.9 1.0 O A:HOH302 2.6 53.3 1.0 CE1 A:HIS172 2.9 29.9 1.0 C4C A:HEC201 3.0 54.6 1.0 C1A A:HEC201 3.1 53.6 1.0 C4A A:HEC201 3.1 50.5 1.0 C1D A:HEC201 3.1 53.6 1.0 C1C A:HEC201 3.1 50.8 1.0 C4D A:HEC201 3.1 53.4 1.0 C1B A:HEC201 3.1 47.7 1.0 C4B A:HEC201 3.1 53.7 1.0 CD2 A:HIS172 3.2 29.9 1.0 CHD A:HEC201 3.4 53.0 1.0 CHA A:HEC201 3.4 47.7 1.0 CHB A:HEC201 3.5 48.2 1.0 CHC A:HEC201 3.5 50.5 1.0 O A:HOH325 3.8 53.3 1.0 ND1 A:HIS172 4.1 29.9 1.0 OE2 A:GLU131 4.2 65.7 0.3 C2A A:HEC201 4.3 46.6 1.0 C3A A:HEC201 4.3 52.0 1.0 CG A:HIS172 4.3 29.9 1.0 C2C A:HEC201 4.3 55.1 1.0 C3C A:HEC201 4.3 54.2 1.0 C2D A:HEC201 4.3 51.1 1.0 C2B A:HEC201 4.3 50.8 1.0 C3B A:HEC201 4.3 50.4 1.0 C3D A:HEC201 4.3 55.0 1.0 CZ A:PHE76 4.6 50.2 1.0 CE2 A:PHE76 4.7 48.8 1.0 OE1 A:GLU131 4.8 68.3 0.3 CD A:GLU131 4.8 66.9 0.3 CE1 A:PHE182 4.9 51.5 1.0

Iron binding site 2 out of 2 in the K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of K106L/A131E Mutant of Cytochrome P460 From Nitrosomonas Sp. AL212 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:62.9 occ:1.00 FE B:HEC201 0.0 62.9 1.0 NC B:HEC201 2.0 71.3 1.0 NA B:HEC201 2.1 71.9 1.0 NB B:HEC201 2.1 72.4 1.0 ND B:HEC201 2.1 71.5 1.0 NE2 B:HIS172 2.2 29.9 1.0 O B:HOH312 2.7 56.3 1.0 CE1 B:HIS172 2.9 29.9 1.0 C1A B:HEC201 3.0 72.1 1.0 C4D B:HEC201 3.1 70.0 1.0 C1C B:HEC201 3.1 70.5 1.0 C4C B:HEC201 3.1 70.6 1.0 C1D B:HEC201 3.1 66.6 1.0 C4B B:HEC201 3.1 69.7 1.0 C4A B:HEC201 3.1 67.5 1.0 C1B B:HEC201 3.1 72.2 1.0 CD2 B:HIS172 3.4 29.9 1.0 CHA B:HEC201 3.4 65.2 1.0 CHD B:HEC201 3.4 67.8 1.0 CHC B:HEC201 3.4 71.8 1.0 CHB B:HEC201 3.5 70.4 1.0 O B:HOH311 3.5 64.5 1.0 ND1 B:HIS172 4.1 29.9 1.0 C2A B:HEC201 4.3 69.3 1.0 C3A B:HEC201 4.3 69.6 1.0 C2C B:HEC201 4.3 67.1 1.0 C3C B:HEC201 4.3 69.4 1.0 C3D B:HEC201 4.3 66.5 1.0 C2D B:HEC201 4.3 67.8 1.0 C3B B:HEC201 4.3 70.6 1.0 C2B B:HEC201 4.3 76.7 1.0 CG B:HIS172 4.4 29.9 1.0 CZ B:PHE76 4.5 75.7 1.0 CE2 B:PHE76 4.7 74.5 1.0

R.E.Coleman, A.C.Vilbert, K.M.Lancaster. The Heme-Lys Cross-Link in Cytochrome P460 Promotes Catalysis By Enforcing Secondary Coordination Sphere Architecture. Biochemistry 2020.
ISSN: ISSN 0006-2960
PubMed: 32525655
DOI: 10.1021/ACS.BIOCHEM.0C00261