Potassium in PDB 4l4e: Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G

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

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G, PDB code: 4l4e 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)	34.55 / 1.26
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.644, 103.594, 106.082, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 21.1

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A/K178G 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 (pdb code 4l4e). 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, PDB code: 4l4e:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:15.8 occ:1.00 OG1 A:THR66 2.7 12.4 1.0 O A:HOH742 2.7 29.2 1.0 O A:LEU45 2.7 12.6 1.0 O A:VAL50 2.8 12.2 1.0 O A:HOH660 2.8 19.8 1.0 O A:PRO51 2.8 12.9 1.0 C A:PRO51 3.5 12.0 1.0 C A:VAL50 3.5 11.4 1.0 CB A:THR66 3.6 11.2 1.0 CB A:VAL50 3.7 12.4 1.0 CG1 A:VAL50 3.8 13.6 1.0 C A:LEU45 3.9 10.5 1.0 NE A:ARG67 3.9 19.4 1.0 N A:ASP52 4.1 12.7 1.0 CG2 A:THR66 4.1 13.1 1.0 NH2 A:ARG67 4.1 31.8 1.0 CA A:GLN46 4.1 12.4 1.0 CA A:ASP52 4.1 12.6 1.0 CA A:VAL50 4.2 12.3 1.0 N A:PRO51 4.3 11.8 1.0 CA A:PRO51 4.4 12.2 1.0 CZ A:ARG67 4.4 24.2 1.0 O A:GLU47 4.4 14.5 1.0 N A:GLN46 4.5 11.4 1.0 C A:GLN46 4.7 13.0 1.0 C A:ASP52 4.7 12.3 1.0 OD2 A:ASP52 4.7 17.2 1.0 O A:ASP52 4.8 13.4 1.0 CG A:ARG67 4.8 19.4 1.0 CD A:ARG67 4.9 20.6 1.0 CA A:THR66 4.9 12.1 1.0 O A:THR66 5.0 14.0 1.0 CG2 A:VAL50 5.0 14.0 1.0 N A:VAL50 5.0 13.4 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:K505 b:19.0 occ:1.00 O A:TYR96 2.6 21.4 1.0 O A:GLU84 2.6 21.1 1.0 O A:HOH964 2.8 36.1 1.0 O A:GLY93 2.8 20.3 1.0 O A:HOH877 2.9 30.2 1.0 O A:GLU94 2.9 23.3 1.0 C A:GLU94 3.5 19.6 1.0 C A:TYR96 3.7 20.8 1.0 CA A:GLU94 3.7 18.9 1.0 C A:GLU84 3.8 20.9 1.0 C A:GLY93 3.9 18.6 1.0 N A:TYR96 4.0 20.3 1.0 CA A:TYR96 4.3 18.2 1.0 N A:GLU94 4.3 19.2 1.0 CG A:GLU84 4.4 33.4 1.0 CB A:TYR96 4.4 18.2 1.0 N A:ALA95 4.5 20.9 1.0 CA A:CYS85 4.5 19.2 1.0 C A:ALA95 4.6 21.6 1.0 N A:CYS85 4.6 18.6 1.0 N A:ASP97 4.8 19.7 1.0 CA A:GLU84 4.9 18.8 1.0 CB A:CYS85 4.9 17.0 1.0 CB A:GLU94 5.0 22.3 1.0 CA A:ALA95 5.0 20.5 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