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Potassium in PDB 2feu: P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX

Enzymatic activity of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX

All present enzymatic activity of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX:
1.14.15.1;

Protein crystallography data

The structure of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX, PDB code: 2feu was solved by K.Von Koenig, T.M.Makris, S.G.Sligar, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.80 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.130, 62.230, 94.710, 90.00, 90.64, 90.00
R / Rfree (%) 21.4 / 23.8

Other elements in 2feu:

The structure of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Potassium Binding Sites:

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

Potassium binding site 1 out of 3 in 2feu

Go back to Potassium Binding Sites List in 2feu
Potassium binding site 1 out of 3 in the P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K729

b:24.2
occ:1.00
O A:TYR96 2.7 24.3 1.0
O A:GLU84 2.7 26.0 1.0
O A:GLY93 2.8 24.0 1.0
O A:GLU94 2.8 25.9 1.0
O A:HOH1534 2.8 25.3 1.0
O A:HOH1608 2.9 32.5 1.0
C A:GLU94 3.4 25.1 1.0
CA A:GLU94 3.6 26.4 1.0
C A:TYR96 3.7 22.7 1.0
C A:GLU84 3.9 24.7 1.0
C A:GLY93 3.9 25.5 1.0
N A:TYR96 4.1 23.4 1.0
O A:HOH1569 4.1 44.9 1.0
N A:GLU94 4.3 25.7 1.0
CA A:TYR96 4.4 23.3 1.0
N A:ALA95 4.4 24.5 1.0
CA A:CYS85 4.5 25.2 1.0
C A:ALA95 4.5 22.9 1.0
N A:CYS85 4.6 25.5 1.0
CB A:TYR96 4.7 23.1 1.0
CG A:GLU84 4.7 30.5 1.0
N A:ASP97 4.7 21.4 1.0
CB A:CYS85 4.9 25.7 1.0
CA A:GLU84 4.9 25.8 1.0
CB A:GLU94 4.9 25.6 1.0
CA A:ASP97 4.9 20.7 1.0
CA A:ALA95 5.0 24.1 1.0

Potassium binding site 2 out of 3 in 2feu

Go back to Potassium Binding Sites List in 2feu
Potassium binding site 2 out of 3 in the P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K728

b:14.3
occ:1.00
O B:GLU84 2.6 12.3 1.0
O B:TYR96 2.7 13.3 1.0
O B:GLY93 2.8 9.4 1.0
O B:GLU94 2.8 9.8 1.0
C B:GLU94 3.4 12.9 1.0
CA B:GLU94 3.7 12.5 1.0
C B:TYR96 3.7 13.0 1.0
C B:GLU84 3.8 13.0 1.0
C B:GLY93 3.9 11.6 1.0
N B:TYR96 4.1 11.4 1.0
N B:GLU94 4.3 11.3 1.0
O B:HOH1650 4.3 29.2 1.0
CG B:GLU84 4.4 24.9 1.0
CA B:TYR96 4.4 11.2 1.0
CA B:CYS85 4.4 12.1 1.0
N B:ALA95 4.4 10.5 1.0
O B:HOH1585 4.5 31.8 1.0
C B:ALA95 4.5 13.1 1.0
N B:CYS85 4.5 12.0 1.0
CB B:TYR96 4.6 12.0 1.0
N B:ASP97 4.8 11.3 1.0
CA B:GLU84 4.8 13.9 1.0
CB B:CYS85 4.9 13.8 1.0
CA B:ALA95 5.0 12.7 1.0
CB B:GLU94 5.0 12.1 1.0
CD B:PRO86 5.0 10.5 1.0

Potassium binding site 3 out of 3 in 2feu

Go back to Potassium Binding Sites List in 2feu
Potassium binding site 3 out of 3 in the P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K730

b:16.2
occ:1.00
O B:VAL18 2.7 17.5 1.0
O B:PRO16 2.8 18.3 1.0
OE2 B:GLU20 2.8 18.3 1.0
O B:PRO15 2.9 18.6 1.0
O B:HOH1448 3.0 17.1 1.0
C B:PRO16 3.4 18.3 1.0
CD2 B:LEU14 3.6 21.8 1.0
C B:VAL18 3.6 16.7 1.0
CA B:PRO16 3.7 18.6 1.0
CD B:GLU20 3.7 18.7 1.0
N B:VAL18 3.9 15.4 1.0
C B:PRO15 3.9 19.5 1.0
CG B:LEU14 4.0 21.0 1.0
O B:HOH1527 4.1 22.1 1.0
OE1 B:GLU20 4.2 20.0 1.0
CA B:VAL18 4.3 16.4 1.0
N B:PRO16 4.3 19.4 1.0
N B:HIS17 4.3 17.1 1.0
O B:HOH1616 4.5 29.7 1.0
C B:HIS17 4.5 15.8 1.0
N B:PRO19 4.7 18.0 1.0
O B:LEU14 4.8 18.7 1.0
CB B:VAL18 4.8 17.1 1.0
CG B:GLU20 4.9 18.6 1.0
CA B:HIS17 4.9 16.9 1.0
N B:GLU20 4.9 18.3 1.0
CA B:PRO19 4.9 18.6 1.0
CB B:LEU14 4.9 20.1 1.0

Reference:

T.M.Makris, K.Von Koenig, I.Schlichting, S.G.Sligar. The Status of High-Valent Metal Oxo Complexes in the P450 Cytochromes. J.Inorg.Biochem. V. 100 507 2006.
ISSN: ISSN 0162-0134
PubMed: 16510191
DOI: 10.1016/J.JINORGBIO.2006.01.025
Page generated: Sun Dec 13 23:09:38 2020

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