Potassium in PDB 4l4a: Structure of L358A/K178G Mutant of P450CAM Bound to Camphor

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

The structure of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4a 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)	29.78 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.436, 103.401, 105.813, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 23.1

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

Iron

(Fe)

1 atom

The binding sites of Potassium atom in the Structure of L358A/K178G Mutant of P450CAM Bound to Camphor (pdb code 4l4a). 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 L358A/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4a:
Jump to Potassium binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:20.2 occ:1.00 O A:TYR96 2.6 33.7 1.0 O A:GLU84 2.7 25.9 1.0 O A:HOH809 2.8 31.6 1.0 O A:HOH818 2.8 35.2 1.0 O A:GLY93 2.8 25.3 1.0 O A:GLU94 2.9 29.4 1.0 C A:GLU94 3.4 26.7 1.0 CA A:GLU94 3.6 24.7 1.0 C A:TYR96 3.7 30.9 1.0 C A:GLY93 3.9 24.1 1.0 C A:GLU84 3.9 24.3 1.0 N A:TYR96 4.0 24.7 1.0 N A:GLU94 4.2 18.7 1.0 CA A:TYR96 4.3 23.6 1.0 N A:ALA95 4.4 30.4 1.0 O A:HOH871 4.5 34.1 1.0 C A:ALA95 4.5 22.9 1.0 CA A:CYS85 4.6 19.4 1.0 CB A:TYR96 4.6 16.8 1.0 CG A:GLU84 4.7 37.8 1.0 N A:CYS85 4.7 22.7 1.0 N A:ASP97 4.7 26.9 1.0 CB A:GLU94 4.9 21.4 1.0 CA A:GLU84 4.9 27.3 1.0 CA A:ASP97 4.9 26.2 1.0 CA A:ALA95 4.9 27.3 1.0

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of L358A/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:25.4 occ:1.00 OG1 A:THR66 2.7 10.9 1.0 O A:LEU45 2.7 11.9 1.0 O A:VAL50 2.8 13.2 1.0 O A:HOH695 2.8 23.9 1.0 O A:HOH666 2.8 29.1 1.0 O A:PRO51 2.9 11.4 1.0 C A:PRO51 3.4 16.4 1.0 C A:VAL50 3.5 12.2 1.0 CB A:THR66 3.5 9.9 1.0 CB A:VAL50 3.6 11.6 1.0 CG1 A:VAL50 3.7 11.1 1.0 C A:LEU45 3.9 14.0 1.0 CG2 A:THR66 4.0 9.8 1.0 N A:ASP52 4.0 13.4 1.0 NE A:ARG67 4.0 32.7 1.0 CA A:ASP52 4.1 12.7 1.0 CA A:GLN46 4.1 10.1 1.0 NH2 A:ARG67 4.1 46.8 1.0 CA A:VAL50 4.2 15.0 1.0 N A:PRO51 4.2 12.5 1.0 CA A:PRO51 4.3 12.7 1.0 CZ A:ARG67 4.4 40.8 1.0 O A:GLU47 4.4 15.0 1.0 N A:GLN46 4.5 11.1 1.0 C A:ASP52 4.7 17.9 1.0 OD2 A:ASP52 4.7 17.6 1.0 C A:GLN46 4.7 14.7 1.0 O A:ASP52 4.8 18.7 1.0 CG2 A:VAL50 4.8 11.4 1.0 CG A:ARG67 4.9 18.6 1.0 CA A:THR66 4.9 9.5 1.0 CD A:ARG67 4.9 21.9 1.0 N A:VAL50 5.0 15.0 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