Potassium in PDB 4l4c: Structure of L358P/K178G Mutant of P450CAM Bound to Camphor

All present enzymatic activity of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor:
1.14.15.1;

The structure of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4c 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)	29.26 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.581, 61.519, 94.964, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 24.3

The structure of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Potassium atom in the Structure of L358P/K178G Mutant of P450CAM Bound to Camphor (pdb code 4l4c). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Structure of L358P/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4c:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Structure of L358P/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 L358P/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:15.8 occ:1.00 O A:GLU84 2.6 13.1 1.0 O A:TYR96 2.8 11.8 1.0 O A:GLU94 2.8 16.9 1.0 O A:HOH641 2.9 14.9 1.0 O A:GLY93 2.9 18.7 1.0 O A:HOH862 3.0 25.0 1.0 C A:GLU94 3.4 17.2 1.0 CA A:GLU94 3.7 22.2 1.0 C A:TYR96 3.8 18.5 1.0 C A:GLU84 3.8 13.6 1.0 C A:GLY93 3.9 15.2 1.0 O A:HOH631 4.1 17.4 1.0 N A:TYR96 4.1 22.5 1.0 N A:GLU94 4.3 12.6 1.0 CA A:TYR96 4.4 19.5 1.0 N A:ALA95 4.5 17.7 1.0 CA A:CYS85 4.5 16.7 1.0 OE2 A:GLU84 4.6 49.4 1.0 C A:ALA95 4.6 20.1 1.0 N A:CYS85 4.6 13.7 1.0 CB A:TYR96 4.6 10.5 1.0 CD A:GLU84 4.7 50.0 1.0 N A:ASP97 4.7 13.7 1.0 CG A:GLU84 4.8 41.5 1.0 O A:HOH874 4.8 27.7 1.0 CA A:GLU84 4.8 17.0 1.0 CA A:ASP97 4.9 14.5 1.0 CB A:GLU94 5.0 14.6 1.0 CA A:ALA95 5.0 23.6 1.0

Potassium binding site 2 out of 3 in the Structure of L358P/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 L358P/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:20.2 occ:1.00 O A:VAL18 2.6 25.9 1.0 O A:HOH655 2.8 12.2 1.0 O A:PRO16 2.9 24.5 1.0 O A:PRO15 3.0 17.6 1.0 C A:PRO16 3.4 22.9 1.0 C A:VAL18 3.6 23.4 1.0 OE2 A:GLU20 3.6 29.6 1.0 CD2 A:LEU14 3.6 18.0 1.0 N A:VAL18 3.7 17.0 1.0 CA A:PRO16 3.7 25.7 1.0 O A:HOH672 3.8 21.2 1.0 C A:PRO15 3.9 17.8 1.0 CG A:LEU14 4.1 24.0 1.0 OE1 A:GLU20 4.1 52.2 1.0 CD A:GLU20 4.2 42.5 1.0 CA A:VAL18 4.2 22.4 1.0 N A:PRO16 4.3 25.8 1.0 N A:HIS17 4.3 18.7 1.0 C A:HIS17 4.5 18.3 1.0 N A:PRO19 4.5 20.7 1.0 O A:HOH728 4.7 24.6 1.0 O A:LEU14 4.7 25.1 1.0 CA A:PRO19 4.8 20.8 1.0 CB A:VAL18 4.8 15.1 1.0 CA A:HIS17 4.9 18.5 1.0 N A:GLU20 4.9 19.5 1.0 CB A:LEU14 4.9 21.2 1.0

Potassium binding site 3 out of 3 in the Structure of L358P/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 3 of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range: probe atom residue distance (Å) B Occ B:K503 b:22.7 occ:1.00 O B:GLU84 2.6 23.1 1.0 O B:TYR96 2.7 20.9 1.0 O B:HOH720 2.9 20.4 1.0 O B:HOH662 2.9 16.1 1.0 O B:GLY93 2.9 20.3 1.0 O B:GLU94 3.1 21.0 1.0 O B:HOH699 3.3 28.6 1.0 C B:GLU94 3.6 21.4 1.0 C B:TYR96 3.7 21.7 1.0 C B:GLU84 3.8 25.3 1.0 CA B:GLU94 3.9 22.1 1.0 N B:TYR96 4.0 22.3 1.0 C B:GLY93 4.0 19.5 1.0 O B:HOH740 4.1 26.4 1.0 CA B:TYR96 4.3 20.4 1.0 CG B:GLU84 4.5 38.6 1.0 N B:GLU94 4.5 18.1 1.0 CB B:TYR96 4.5 19.8 1.0 N B:ALA95 4.5 23.7 1.0 C B:ALA95 4.6 22.4 1.0 CA B:CYS85 4.6 17.4 1.0 N B:CYS85 4.6 17.6 1.0 N B:ASP97 4.7 18.0 1.0 CA B:GLU84 4.7 22.7 1.0 CA B:ASP97 5.0 15.7 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