Potassium in PDB 6we6: Camphor Bound P450CAM D251E Structure

All present enzymatic activity of Camphor Bound P450CAM D251E Structure:
1.14.15.1;

The structure of Camphor Bound P450CAM D251E Structure, PDB code: 6we6 was solved by J.A.Amaya, T.L.Poulos, D.Batabyal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.36 / 2.16
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.657, 62.204, 224.184, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 25.6

The structure of Camphor Bound P450CAM D251E Structure also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Potassium atom in the Camphor Bound P450CAM D251E Structure (pdb code 6we6). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Camphor Bound P450CAM D251E Structure, PDB code: 6we6:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Camphor Bound P450CAM D251E Structure


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Camphor Bound P450CAM D251E Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:28.0 occ:1.00 O A:GLU84 2.6 23.2 1.0 O A:TYR96 2.7 25.4 1.0 O A:HOH767 2.8 36.3 1.0 O A:GLY93 2.8 21.2 1.0 O A:GLU94 2.9 25.1 1.0 O A:HOH763 2.9 36.3 1.0 C A:GLU94 3.5 26.6 1.0 CA A:GLU94 3.7 26.5 1.0 C A:TYR96 3.8 24.9 1.0 C A:GLU84 3.8 26.6 1.0 C A:GLY93 3.9 24.6 1.0 N A:TYR96 4.1 23.3 1.0 N A:GLU94 4.3 25.7 1.0 CG A:GLU84 4.3 40.4 1.0 CA A:TYR96 4.3 22.8 1.0 CA A:CYS85 4.5 26.6 1.0 N A:ALA95 4.5 22.2 1.0 C A:ALA95 4.5 27.7 1.0 CB A:TYR96 4.5 21.8 1.0 N A:CYS85 4.6 20.9 1.0 N A:ASP97 4.8 24.1 1.0 CB A:CYS85 4.8 25.9 1.0 CA A:GLU84 4.9 25.6 1.0 O A:ALA95 5.0 26.6 1.0 CA A:ALA95 5.0 23.1 1.0

Potassium binding site 2 out of 2 in the Camphor Bound P450CAM D251E Structure


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Camphor Bound P450CAM D251E Structure within 5.0Å range: probe atom residue distance (Å) B Occ B:K503 b:44.1 occ:1.00 O B:GLU84 2.6 41.1 1.0 O B:TYR96 2.7 38.5 1.0 O B:HOH692 2.8 40.1 1.0 O B:GLU94 2.9 38.6 1.0 O B:GLY93 3.0 36.9 1.0 C B:GLU94 3.6 41.6 1.0 C B:TYR96 3.7 38.4 1.0 C B:GLU84 3.8 40.9 1.0 CA B:GLU94 3.9 43.7 1.0 C B:GLY93 4.1 40.2 1.0 N B:TYR96 4.1 38.3 1.0 CA B:TYR96 4.4 40.4 1.0 CA B:CYS85 4.4 36.3 1.0 C B:ALA95 4.5 42.2 1.0 N B:GLU94 4.5 41.6 1.0 N B:ALA95 4.6 37.3 1.0 N B:CYS85 4.6 35.6 1.0 CB B:TYR96 4.7 36.8 1.0 N B:ASP97 4.7 39.2 1.0 CB B:CYS85 4.8 40.0 1.0 CA B:GLU84 4.9 39.8 1.0 CA B:ASP97 4.9 35.9 1.0 O B:ALA95 5.0 40.3 1.0

J.A.Amaya, D.Batabyal, T.L.Poulos. Proton Relay Network in the Bacterial P450S: CYP101A1 and CYP101D1. Biochemistry V. 59 2896 2020.
ISSN: ISSN 0006-2960
PubMed: 32574066
DOI: 10.1021/ACS.BIOCHEM.0C00329