Potassium in PDB 1dz6: Ferrous P450CAM From Pseudomonas Putida

The structure of Ferrous P450CAM From Pseudomonas Putida, PDB code: 1dz6 was solved by I.Schlichting, J.Berendzen, K.Chu, A.M.Stock, S.A.Maves, D.E.Benson, R.M.Sweet, D.Ringe, G.A.Petsko, S.G.Sligar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.800, 62.800, 95.500, 90.00, 90.60, 90.00
R / Rfree (%)	18.8 / 26.8

The structure of Ferrous P450CAM From Pseudomonas Putida also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Potassium atom in the Ferrous P450CAM From Pseudomonas Putida (pdb code 1dz6). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Ferrous P450CAM From Pseudomonas Putida, PDB code: 1dz6:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Ferrous P450CAM From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ferrous P450CAM From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:21.0 occ:1.00 O A:GLU84 2.7 23.9 1.0 O A:TYR96 2.8 17.2 1.0 O A:HOH864 2.8 32.8 1.0 O A:GLY93 2.9 18.4 1.0 O A:HOH847 2.9 29.2 1.0 O A:GLU94 3.0 19.2 1.0 C A:GLU94 3.5 19.5 1.0 CA A:GLU94 3.7 25.8 1.0 C A:TYR96 3.8 23.2 1.0 C A:GLU84 3.9 21.2 1.0 C A:GLY93 3.9 18.9 1.0 O A:HOH851 4.1 39.5 1.0 N A:TYR96 4.1 20.3 1.0 N A:GLU94 4.3 25.1 1.0 CA A:CYS85 4.3 21.9 1.0 CA A:TYR96 4.4 15.7 1.0 C A:ALA95 4.5 16.6 1.0 N A:ALA95 4.6 20.1 1.0 N A:CYS85 4.6 21.8 1.0 CB A:TYR96 4.6 25.7 1.0 CB A:CYS85 4.7 28.8 1.0 N A:ASP97 4.8 24.5 1.0 CG A:GLU84 4.8 53.0 1.0 O A:HOH797 4.8 34.5 1.0 CA A:GLU84 4.9 26.1 1.0 CD A:PRO86 5.0 17.3 1.0

Potassium binding site 2 out of 3 in the Ferrous P450CAM From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ferrous P450CAM From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ B:K503 b:13.0 occ:1.00 O B:HOH916 2.7 24.6 1.0 O B:GLU84 2.7 11.6 1.0 O B:GLY93 2.8 12.5 1.0 O B:TYR96 2.8 15.7 1.0 O B:HOH910 2.8 21.6 1.0 O B:GLU94 2.8 7.1 1.0 C B:GLU94 3.5 14.7 1.0 CA B:GLU94 3.6 19.2 1.0 C B:TYR96 3.8 17.8 1.0 C B:GLY93 3.8 13.2 1.0 C B:GLU84 3.9 12.8 1.0 N B:TYR96 4.2 16.1 1.0 N B:GLU94 4.2 19.1 1.0 O B:HOH658 4.3 32.1 1.0 CA B:TYR96 4.4 13.0 1.0 N B:ALA95 4.5 11.0 1.0 CA B:CYS85 4.5 15.6 1.0 O B:HOH957 4.5 46.7 1.0 CG B:GLU84 4.5 20.9 1.0 C B:ALA95 4.6 19.6 1.0 O B:HOH626 4.7 26.5 1.0 N B:CYS85 4.7 9.2 1.0 CB B:TYR96 4.7 13.2 1.0 N B:ASP97 4.8 6.8 1.0 CA B:GLU84 4.9 10.3 1.0 CB B:CYS85 4.9 11.3 1.0 CB B:GLU94 4.9 13.3 1.0 CD B:PRO86 5.0 7.4 1.0 CA B:ASP97 5.0 6.8 1.0

Potassium binding site 3 out of 3 in the Ferrous P450CAM From Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Ferrous P450CAM From Pseudomonas Putida within 5.0Å range: probe atom residue distance (Å) B Occ B:K504 b:19.0 occ:1.00 O B:VAL18 2.8 14.7 1.0 O B:PRO16 2.9 20.1 1.0 O B:HOH691 3.0 16.2 1.0 O B:PRO15 3.0 16.6 1.0 OE2 B:GLU20 3.0 16.2 1.0 C B:PRO16 3.5 15.6 1.0 CD2 B:LEU14 3.6 24.4 1.0 CD B:GLU20 3.8 13.8 1.0 CA B:PRO16 3.8 19.5 1.0 C B:VAL18 3.8 15.2 1.0 O B:HOH613 4.0 22.6 1.0 C B:PRO15 4.0 12.7 1.0 OE1 B:GLU20 4.0 17.4 1.0 N B:VAL18 4.1 17.4 1.0 CG B:LEU14 4.1 24.4 1.0 N B:PRO16 4.3 22.1 1.0 N B:HIS17 4.4 11.9 1.0 CA B:VAL18 4.5 16.2 1.0 C B:HIS17 4.6 5.9 1.0 N B:PRO19 4.7 20.2 1.0 O B:LEU14 4.7 22.5 1.0 CA B:PRO19 4.8 22.7 1.0 CG B:GLU20 4.8 15.1 1.0 N B:GLU20 4.9 21.2 1.0 CA B:HIS17 4.9 11.0 1.0 CB B:VAL18 4.9 8.9 1.0

I.Schlichting, J.Berendzen, K.Chu, A.M.Stock, S.A.Maves, D.E.Benson, R.M.Sweet, D.Ringe, G.A.Petsko, S.G.Sligar. The Catalytic Pathway of Cytochrome P450CAM at Atomic Resolution Science V. 287 1615 2000.
ISSN: ISSN 0036-8075
PubMed: 10698731
DOI: 10.1126/SCIENCE.287.5458.1615