Potassium in PDB 4l4b: Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor

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

The structure of Structure of L358A/K178G/D182N Mutant of P450CAM Bound to Camphor, PDB code: 4l4b 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)	34.51 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.503, 103.587, 105.843, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 23.5

The structure of Structure of L358A/K178G/D182N 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/D182N Mutant of P450CAM Bound to Camphor (pdb code 4l4b). 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/D182N Mutant of P450CAM Bound to Camphor, PDB code: 4l4b:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of L358A/K178G/D182N 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/D182N Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:27.0 occ:1.00 O A:TYR96 2.7 34.3 1.0 O A:GLU84 2.7 29.5 1.0 O A:GLU94 2.7 35.7 1.0 O A:GLY93 2.8 26.4 1.0 O A:HOH855 2.8 30.3 1.0 O A:HOH782 2.9 30.1 1.0 C A:GLU94 3.3 33.5 1.0 CA A:GLU94 3.5 28.6 1.0 C A:TYR96 3.7 34.8 1.0 C A:GLY93 3.8 26.6 1.0 C A:GLU84 3.9 31.4 1.0 N A:TYR96 4.0 31.4 1.0 N A:GLU94 4.1 22.6 1.0 N A:ALA95 4.3 36.2 1.0 CA A:TYR96 4.3 29.8 1.0 C A:ALA95 4.4 31.9 1.0 CA A:CYS85 4.5 21.6 1.0 CB A:TYR96 4.6 28.6 1.0 CG A:GLU84 4.7 45.4 1.0 N A:CYS85 4.7 31.5 1.0 N A:ASP97 4.7 34.2 1.0 CB A:GLU94 4.8 29.2 1.0 CA A:ALA95 4.9 34.0 1.0 O A:ALA95 4.9 30.7 1.0 CA A:ASP97 4.9 33.1 1.0

Potassium binding site 2 out of 2 in the Structure of L358A/K178G/D182N 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/D182N Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:25.2 occ:1.00 OG1 A:THR66 2.7 11.9 1.0 O A:HOH639 2.7 24.3 1.0 O A:PRO51 2.7 12.7 1.0 O A:LEU45 2.8 14.0 1.0 O A:VAL50 2.8 17.8 1.0 O A:HOH666 2.9 31.1 1.0 C A:PRO51 3.4 15.8 1.0 C A:VAL50 3.5 16.1 1.0 CB A:THR66 3.5 11.5 1.0 CB A:VAL50 3.7 12.0 1.0 CG1 A:VAL50 3.7 12.8 1.0 NE A:ARG67 3.9 36.0 1.0 C A:LEU45 4.0 16.5 1.0 N A:ASP52 4.0 22.2 1.0 CG2 A:THR66 4.0 11.7 1.0 CA A:ASP52 4.1 17.6 1.0 NH2 A:ARG67 4.1 43.9 1.0 CA A:GLN46 4.1 13.8 1.0 N A:PRO51 4.2 13.1 1.0 CA A:VAL50 4.2 12.5 1.0 CA A:PRO51 4.3 16.0 1.0 O A:GLU47 4.4 15.5 1.0 CZ A:ARG67 4.4 40.9 1.0 N A:GLN46 4.5 15.5 1.0 C A:ASP52 4.6 19.0 1.0 OD2 A:ASP52 4.7 17.2 1.0 O A:ASP52 4.7 19.8 1.0 C A:GLN46 4.7 16.4 1.0 CG A:ARG67 4.8 26.9 1.0 CA A:THR66 4.9 11.6 1.0 CD A:ARG67 4.9 30.2 1.0 CG2 A:VAL50 4.9 11.8 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