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Potassium in PDB 6cp4: P450CAM D251N Mutant

Enzymatic activity of P450CAM D251N Mutant

All present enzymatic activity of P450CAM D251N Mutant:
1.14.15.1;

Protein crystallography data

The structure of P450CAM D251N Mutant, PDB code: 6cp4 was solved by H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.600, 103.200, 36.500, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 27

Other elements in 6cp4:

The structure of P450CAM D251N Mutant also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the P450CAM D251N Mutant (pdb code 6cp4). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the P450CAM D251N Mutant, PDB code: 6cp4:

Potassium binding site 1 out of 1 in 6cp4

Go back to Potassium Binding Sites List in 6cp4
Potassium binding site 1 out of 1 in the P450CAM D251N Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of P450CAM D251N Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K500

b:23.0
occ:1.00
O A:HOH818 2.5 45.4 1.0
O A:TYR96 2.5 21.7 1.0
O A:GLU84 2.7 25.3 1.0
O A:GLY93 2.8 20.5 1.0
O A:GLU94 2.9 27.2 1.0
H2 A:HOH818 2.9 0.0 1.0
O A:HOH767 3.0 33.0 1.0
H1 A:HOH818 3.4 0.0 1.0
C A:GLU94 3.4 24.5 1.0
H2 A:HOH767 3.4 0.0 1.0
CA A:GLU94 3.6 25.2 1.0
C A:TYR96 3.7 22.1 1.0
H1 A:HOH767 3.7 0.0 1.0
C A:GLY93 3.9 20.8 1.0
C A:GLU84 3.9 24.9 1.0
H A:TYR96 4.1 0.0 1.0
N A:TYR96 4.2 23.0 1.0
N A:GLU94 4.2 21.5 1.0
CA A:TYR96 4.4 21.4 1.0
N A:ALA95 4.5 22.7 1.0
CA A:CYS85 4.6 18.7 1.0
CB A:TYR96 4.6 19.4 1.0
C A:ALA95 4.6 22.9 1.0
N A:CYS85 4.7 22.5 1.0
N A:ASP97 4.7 19.1 1.0
CG A:GLU84 4.8 39.8 1.0
CB A:GLU94 4.9 27.5 1.0
CA A:ASP97 4.9 18.7 1.0
CA A:GLU84 4.9 26.2 1.0

Reference:

M.Vidakovic, S.G.Sligar, H.Li, T.L.Poulos. Understanding the Role of the Essential ASP251 in Cytochrome P450CAM Using Site-Directed Mutagenesis, Crystallography, and Kinetic Solvent Isotope Effect. Biochemistry V. 37 9211 1998.
ISSN: ISSN 0006-2960
PubMed: 9649301
DOI: 10.1021/BI980189F
Page generated: Mon Aug 12 15:35:30 2024

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