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Potassium in PDB 2zwu: Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM

Enzymatic activity of Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM

All present enzymatic activity of Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM, PDB code: 2zwu was solved by K.Sakurai, H.Shimada, T.Hayashi, T.Tsukihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.90 / 1.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 63.608, 63.608, 250.389, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 18.4

Other elements in 2zwu:

The structure of Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM (pdb code 2zwu). 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 Camphor Soaked Ferric Cytochrome P450CAM, PDB code: 2zwu:

Potassium binding site 1 out of 1 in 2zwu

Go back to Potassium Binding Sites List in 2zwu
Potassium binding site 1 out of 1 in the Crystal Structure of Camphor Soaked Ferric Cytochrome P450CAM


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 Camphor Soaked Ferric Cytochrome P450CAM within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K424

b:9.6
occ:1.00
O A:GLU84 2.6 10.5 1.0
O A:TYR96 2.6 10.1 1.0
O A:GLY93 2.8 8.7 1.0
O A:HOH1389 2.8 22.1 1.0
O A:GLU94 2.8 10.7 1.0
O A:HOH1382 2.9 16.6 1.0
HA A:GLU94 3.1 9.6 1.0
C A:GLU94 3.4 9.7 1.0
HA A:CYS85 3.7 9.5 0.9
HA A:CYS85 3.7 9.6 0.1
CA A:GLU94 3.7 9.4 1.0
C A:TYR96 3.7 9.0 1.0
C A:GLU84 3.8 10.2 1.0
C A:GLY93 3.8 8.7 1.0
H A:TYR96 4.1 9.3 1.0
N A:TYR96 4.1 9.4 1.0
N A:GLU94 4.3 8.8 1.0
SG A:CYS85 4.3 11.7 0.1
HA A:ASP97 4.4 9.3 1.0
O A:HOH1312 4.4 33.1 1.0
CA A:TYR96 4.4 8.9 1.0
CA A:CYS85 4.4 9.5 0.9
CA A:CYS85 4.5 9.7 0.1
N A:ALA95 4.5 9.4 1.0
CG A:GLU84 4.5 11.4 0.4
C A:ALA95 4.5 9.5 1.0
N A:CYS85 4.6 9.2 1.0
CB A:TYR96 4.6 8.5 1.0
HA A:GLU84 4.7 10.1 0.4
HA A:GLU84 4.7 10.2 0.6
O A:HOH1396 4.7 34.4 1.0
N A:ASP97 4.8 8.8 1.0
CA A:GLU84 4.8 10.0 0.4
CA A:GLU84 4.9 10.0 0.6
O A:HOH1355 4.9 27.6 1.0
CD A:PRO86 4.9 8.8 1.0
CB A:CYS85 4.9 9.7 0.9
CA A:ASP97 5.0 9.3 1.0
O A:ALA95 5.0 10.2 1.0
CB A:GLU94 5.0 10.6 1.0
CA A:ALA95 5.0 9.8 1.0

Reference:

K.Sakurai, H.Shimada, T.Hayashi, T.Tsukihara. Substrate Binding Induces Structural Changes in Cytochrome P450CAM Acta Crystallogr.,Sect.F V. 65 80 2009.
ISSN: ESSN 1744-3091
PubMed: 19193991
DOI: 10.1107/S1744309108044114
Page generated: Sat Aug 9 04:30:03 2025

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