Potassium in PDB 1t88: Crystal Structure of the Ferrous Cytochrome P450CAM (C334A)

All present enzymatic activity of Crystal Structure of the Ferrous Cytochrome P450CAM (C334A):
1.14.15.1;

The structure of Crystal Structure of the Ferrous Cytochrome P450CAM (C334A), PDB code: 1t88 was solved by S.Nagano, T.Tosha, K.Ishimori, I.Morishima, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.66 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	66.990, 62.390, 94.970, 90.00, 89.57, 90.00
R / Rfree (%)	18.7 / 21.2

The structure of Crystal Structure of the Ferrous Cytochrome P450CAM (C334A) also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Potassium atom in the Crystal Structure of the Ferrous Cytochrome P450CAM (C334A) (pdb code 1t88). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of the Ferrous Cytochrome P450CAM (C334A), PDB code: 1t88:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Crystal Structure of the Ferrous Cytochrome P450CAM (C334A)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Ferrous Cytochrome P450CAM (C334A) within 5.0Å range: probe atom residue distance (Å) B Occ A:K1515 b:13.9 occ:1.00 O A:GLU84 2.7 15.0 1.0 O A:TYR96 2.8 15.1 1.0 O A:GLY93 2.9 13.2 1.0 O A:GLU94 3.0 14.4 1.0 O A:HOH1902 3.3 54.5 1.0 C A:GLU94 3.5 15.1 1.0 O A:HOH1973 3.7 36.8 1.0 CA A:GLU94 3.7 14.9 1.0 C A:TYR96 3.9 13.4 1.0 C A:GLU84 3.9 17.0 1.0 C A:GLY93 4.0 15.3 1.0 O A:HOH1946 4.2 32.8 1.0 N A:TYR96 4.3 15.0 1.0 N A:GLU94 4.3 16.6 1.0 CA A:CYS85 4.5 15.0 1.0 CG A:GLU84 4.5 27.3 1.0 N A:ALA95 4.5 14.1 1.0 CA A:TYR96 4.5 13.0 1.0 C A:ALA95 4.6 15.2 1.0 N A:CYS85 4.6 11.8 1.0 CB A:TYR96 4.8 11.8 1.0 N A:ASP97 4.8 11.2 1.0 O A:HOH1843 4.9 27.6 1.0 CA A:GLU84 4.9 14.2 1.0 CD A:PRO86 5.0 13.4 1.0 CA A:ASP97 5.0 13.1 1.0 CB A:GLU94 5.0 16.4 1.0

Potassium binding site 2 out of 3 in the Crystal Structure of the Ferrous Cytochrome P450CAM (C334A)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Ferrous Cytochrome P450CAM (C334A) within 5.0Å range: probe atom residue distance (Å) B Occ A:K1715 b:19.6 occ:1.00 O A:VAL18 2.9 18.4 1.0 OE2 A:GLU20 3.0 21.6 1.0 O A:PRO15 3.0 17.9 1.0 O A:PRO16 3.0 19.1 1.0 O A:HOH1728 3.1 19.0 1.0 C A:PRO16 3.5 18.7 1.0 CA A:PRO16 3.7 17.9 1.0 C A:VAL18 3.7 19.4 1.0 CD2 A:LEU14 3.8 19.9 1.0 CD A:GLU20 3.8 20.7 1.0 O A:HOH1841 3.9 23.1 1.0 C A:PRO15 3.9 18.6 1.0 N A:VAL18 4.0 16.0 1.0 CG A:LEU14 4.0 19.6 1.0 OE1 A:GLU20 4.1 20.3 1.0 N A:PRO16 4.3 18.9 1.0 N A:HIS17 4.3 17.7 1.0 CA A:VAL18 4.4 17.1 1.0 C A:HIS17 4.6 14.3 1.0 O A:LEU14 4.6 21.4 1.0 N A:PRO19 4.7 20.6 1.0 CB A:VAL18 4.9 16.1 1.0 CA A:HIS17 4.9 16.9 1.0 N A:GLU20 4.9 21.7 1.0 CA A:PRO19 4.9 21.7 1.0 CB A:LEU14 5.0 19.2 1.0 CG A:GLU20 5.0 18.7 1.0

Potassium binding site 3 out of 3 in the Crystal Structure of the Ferrous Cytochrome P450CAM (C334A)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of the Ferrous Cytochrome P450CAM (C334A) within 5.0Å range: probe atom residue distance (Å) B Occ B:K2515 b:22.7 occ:1.00 O B:GLU84 2.8 23.5 1.0 O B:TYR96 2.9 18.1 1.0 O B:GLU94 3.0 21.6 1.0 O B:GLY93 3.1 20.7 1.0 O B:HOH2635 3.3 53.7 1.0 C B:GLU94 3.6 21.7 1.0 CA B:GLU94 3.8 24.4 1.0 C B:TYR96 3.9 20.7 1.0 C B:GLU84 3.9 25.8 1.0 C B:GLY93 4.1 23.8 1.0 N B:TYR96 4.3 22.5 1.0 N B:GLU94 4.4 25.1 1.0 N B:ALA95 4.5 21.7 1.0 CA B:TYR96 4.5 19.5 1.0 CG B:GLU84 4.6 41.5 1.0 CA B:CYS85 4.6 23.4 1.0 C B:ALA95 4.6 22.6 1.0 N B:CYS85 4.7 25.6 1.0 CB B:TYR96 4.8 21.0 1.0 N B:ASP97 4.9 18.9 1.0 CA B:GLU84 4.9 26.4 1.0

S.Nagano, T.Tosha, K.Ishimori, I.Morishima, T.L.Poulos. Crystal Structure of the Cytochrome P450CAM Mutant That Exhibits the Same Spectral Perturbations Induced By Putidaredoxin Binding. J.Biol.Chem. V. 279 42844 2004.
ISSN: ISSN 0021-9258
PubMed: 15269210
DOI: 10.1074/JBC.M404217200