Potassium in PDB 4l4d: Structure of Cyanide and Camphor Bound P450CAM Mutant L358A

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

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A, PDB code: 4l4d 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)	34.52 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.614, 103.586, 105.733, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 24

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A 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 (pdb code 4l4d). 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, PDB code: 4l4d:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:21.3 occ:1.00 O A:TYR96 2.6 20.3 1.0 O A:GLU84 2.7 17.3 1.0 O A:HOH1000 2.7 16.6 1.0 O A:GLY93 2.8 18.7 1.0 O A:HOH1001 2.8 67.3 1.0 O A:GLU94 3.0 22.0 1.0 C A:GLU94 3.5 20.2 1.0 C A:TYR96 3.7 19.9 1.0 CA A:GLU94 3.8 14.9 1.0 C A:GLU84 3.9 16.3 1.0 C A:GLY93 3.9 16.9 1.0 N A:TYR96 4.0 23.5 1.0 N A:GLU94 4.3 13.8 1.0 CA A:TYR96 4.3 20.5 1.0 N A:ALA95 4.5 22.5 1.0 C A:ALA95 4.5 28.0 1.0 CA A:CYS85 4.6 13.5 1.0 CB A:TYR96 4.6 23.3 1.0 N A:CYS85 4.7 13.2 1.0 N A:ASP97 4.8 20.6 1.0 CA A:GLU84 4.9 23.0 1.0 CA A:ASP97 5.0 24.2 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:K505 b:15.8 occ:1.00 OG1 A:THR66 2.7 7.9 1.0 O A:VAL50 2.8 8.9 1.0 O A:LEU45 2.8 13.2 1.0 O A:PRO51 2.8 8.9 1.0 O A:HOH743 2.8 18.0 1.0 O A:HOH656 2.8 27.2 1.0 C A:PRO51 3.5 9.7 1.0 C A:VAL50 3.5 9.4 1.0 CB A:THR66 3.5 11.6 1.0 CB A:VAL50 3.7 8.3 1.0 CG1 A:VAL50 3.7 9.0 1.0 NE A:ARG67 3.9 30.7 1.0 C A:LEU45 3.9 17.9 1.0 CG2 A:THR66 4.0 7.0 1.0 NH2 A:ARG67 4.1 35.6 1.0 N A:ASP52 4.1 11.7 1.0 CA A:GLN46 4.1 10.1 1.0 CA A:ASP52 4.2 12.9 1.0 N A:PRO51 4.2 9.1 1.0 CA A:VAL50 4.2 8.9 1.0 CA A:PRO51 4.3 9.2 1.0 CZ A:ARG67 4.4 32.8 1.0 O A:GLU47 4.5 9.1 1.0 N A:GLN46 4.5 7.4 1.0 C A:ASP52 4.7 12.4 1.0 O A:ASP52 4.8 10.8 1.0 OD2 A:ASP52 4.8 9.5 1.0 C A:GLN46 4.8 14.1 1.0 CG A:ARG67 4.8 26.6 1.0 CD A:ARG67 4.9 28.5 1.0 CA A:THR66 4.9 8.7 1.0 CG2 A:VAL50 4.9 11.0 1.0 O A:HOH958 5.0 18.7 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