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Potassium in PDB 2z97: Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin

Enzymatic activity of Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin

All present enzymatic activity of Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin, PDB code: 2z97 was solved by T.Hayashi, K.Harada, K.Sakurai, S.Hirota, H.Shimada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.63 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.493, 66.124, 104.882, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 20.3

Other elements in 2z97:

The structure of Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin (pdb code 2z97). 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 Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin, PDB code: 2z97:

Potassium binding site 1 out of 1 in 2z97

Go back to Potassium Binding Sites List in 2z97
Potassium binding site 1 out of 1 in the Crystal Structure of Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin


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 Ferric Cytochrome P450CAM Reconstituted with 7- Methyl-7-Depropionated Hemin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K415

b:17.6
occ:1.00
 O A:GLU84 2.6 15.8 1.0
O A:TYR96 2.6 18.2 1.0
O A:HOH695 2.7 30.5 1.0
O A:GLY93 2.8 16.7 1.0
O A:GLU94 2.8 17.9 1.0
O A:HOH585 2.9 23.9 1.0
C A:GLU94 3.5 18.4 1.0
OE1 A:GLU84 3.5 21.9 0.4
C A:TYR96 3.7 16.5 1.0
CA A:GLU94 3.7 18.0 1.0
C A:GLU84 3.8 16.0 1.0
C A:GLY93 3.9 17.2 1.0
N A:TYR96 4.0 17.9 1.0
O A:HOH699 4.1 45.4 1.0
N A:GLU94 4.3 17.3 1.0
CA A:TYR96 4.4 16.9 1.0
N A:ALA95 4.5 18.4 1.0
CA A:CYS85 4.5 15.8 1.0
C A:ALA95 4.5 18.5 1.0
CD A:GLU84 4.6 21.1 0.4
N A:CYS85 4.6 15.6 1.0
CB A:TYR96 4.7 16.9 1.0
N A:ASP97 4.7 14.9 1.0
CA A:GLU84 4.9 15.3 1.0
CA A:ASP97 4.9 13.8 1.0
CB A:CYS85 5.0 16.1 1.0
CA A:ALA95 5.0 18.7 1.0

Reference:

T.Hayashi, K.Harada, K.Sakurai, H.Shimada, S.Hirota. A Role of the Heme-7-Propionate Side Chain in Cytochrome P450CAM As A Gate For Regulating the Access of Water Molecules to the Substrate-Binding Site J.Am.Chem.Soc. V. 131 1398 2009.
ISSN: ISSN 0002-7863
PubMed: 19133773
DOI: 10.1021/JA807420K
Page generated: Sun Dec 13 23:14:07 2020

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