Potassium in PDB 4l4f: Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N

All present enzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N:
1.14.15.1;

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N, PDB code: 4l4f was solved by D.Batabyal, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.45 / 1.29
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.565, 103.413, 106.043, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 21.5

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Potassium atom in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N (pdb code 4l4f). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N, PDB code: 4l4f:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:20.6 occ:1.00 O A:GLU84 2.6 22.1 1.0 O A:TYR96 2.6 23.3 1.0 O A:GLY93 2.8 22.0 1.0 O A:HOH1108 2.8 32.7 1.0 O A:GLU94 2.9 23.7 1.0 C A:GLU94 3.4 21.5 1.0 CA A:GLU94 3.7 21.9 1.0 C A:TYR96 3.7 22.2 1.0 C A:GLU84 3.8 20.2 1.0 C A:GLY93 3.9 19.9 1.0 N A:TYR96 4.0 23.0 1.0 N A:GLU94 4.3 21.3 1.0 CA A:TYR96 4.3 20.5 1.0 N A:ALA95 4.4 22.2 1.0 CB A:TYR96 4.4 19.6 1.0 CA A:CYS85 4.4 20.5 1.0 N A:CYS85 4.6 20.3 1.0 C A:ALA95 4.6 25.6 1.0 N A:ASP97 4.8 21.1 1.0 CA A:GLU84 4.8 18.6 1.0 CB A:CYS85 4.9 20.2 1.0 CB A:GLU94 4.9 23.9 1.0 CA A:ALA95 5.0 25.3 1.0

Potassium binding site 2 out of 2 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G/D182N within 5.0Å range: probe atom residue distance (Å) B Occ A:K505 b:16.8 occ:1.00 OG1 A:THR66 2.7 13.3 1.0 O A:LEU45 2.8 13.1 1.0 O A:HOH668 2.8 22.4 1.0 O A:VAL50 2.8 13.7 1.0 O A:PRO51 2.8 13.8 1.0 O A:HOH726 2.9 26.4 1.0 C A:PRO51 3.5 12.7 1.0 C A:VAL50 3.5 12.7 1.0 CB A:THR66 3.6 13.1 1.0 CB A:VAL50 3.7 13.6 1.0 CG1 A:VAL50 3.8 13.8 1.0 NE A:ARG67 3.9 21.9 1.0 C A:LEU45 3.9 12.2 1.0 NH2 A:ARG67 4.0 33.5 1.0 CA A:GLN46 4.1 13.9 1.0 CG2 A:THR66 4.1 16.0 1.0 N A:ASP52 4.1 14.1 1.0 CA A:ASP52 4.2 14.6 1.0 CA A:VAL50 4.3 13.2 1.0 CZ A:ARG67 4.3 24.8 1.0 N A:PRO51 4.3 12.7 1.0 CA A:PRO51 4.4 13.9 1.0 O A:GLU47 4.4 15.2 1.0 N A:GLN46 4.5 13.0 1.0 C A:GLN46 4.7 13.8 1.0 OD2 A:ASP52 4.7 18.6 1.0 C A:ASP52 4.8 13.9 1.0 CG A:ARG67 4.8 19.1 1.0 O A:ASP52 4.8 14.2 1.0 CD A:ARG67 4.8 20.6 1.0 O A:HOH1044 4.9 22.5 1.0 CA A:THR66 4.9 12.9 1.0 O A:THR66 4.9 15.3 1.0 N A:VAL50 5.0 13.5 1.0

D.Batabyal, H.Li, T.L.Poulos. Synergistic Effects of Mutations in Cytochrome P450CAM Designed to Mimic CYP101D1. Biochemistry V. 52 5396 2013.
ISSN: ISSN 0006-2960
PubMed: 23865948
DOI: 10.1021/BI400676D