Atomistry » Potassium » PDB 2xo1-3atv » 2zwt
Atomistry »
  Potassium »
    PDB 2xo1-3atv »
      2zwt »

Potassium in PDB 2zwt: Crystal Structure of Ferric Cytochrome P450CAM

Enzymatic activity of Crystal Structure of Ferric Cytochrome P450CAM

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

Protein crystallography data

The structure of Crystal Structure of Ferric Cytochrome P450CAM, PDB code: 2zwt 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) 23.06 / 1.35
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 63.860, 63.860, 247.304, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 19

Other elements in 2zwt:

The structure of Crystal Structure of 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 Ferric Cytochrome P450CAM (pdb code 2zwt). 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, PDB code: 2zwt:

Potassium binding site 1 out of 1 in 2zwt

Go back to Potassium Binding Sites List in 2zwt
Potassium binding site 1 out of 1 in the Crystal Structure of 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 Ferric Cytochrome P450CAM within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K424

b:10.9
occ:1.00
O A:GLU84 2.6 12.2 1.0
O A:TYR96 2.6 10.2 1.0
O A:GLY93 2.8 9.9 1.0
O A:HOH1382 2.8 21.1 1.0
O A:HOH1389 2.8 26.6 1.0
O A:GLU94 2.9 12.7 1.0
HA A:GLU94 3.1 11.4 1.0
C A:GLU94 3.5 11.4 1.0
HA A:CYS85 3.7 10.5 0.9
HA A:CYS85 3.7 10.5 0.1
CA A:GLU94 3.7 11.4 1.0
C A:TYR96 3.7 9.8 1.0
C A:GLU84 3.8 11.0 1.0
C A:GLY93 3.9 10.3 1.0
O A:HOH1832 4.1 38.0 1.0
H A:TYR96 4.1 10.5 1.0
N A:TYR96 4.1 10.4 1.0
N A:GLU94 4.3 10.5 1.0
SG A:CYS85 4.3 11.2 0.1
HA A:ASP97 4.3 9.9 1.0
CA A:TYR96 4.4 9.8 1.0
CA A:CYS85 4.4 10.0 0.9
CA A:CYS85 4.4 10.5 0.1
N A:ALA95 4.5 11.1 1.0
C A:ALA95 4.5 11.3 1.0
CG A:GLU84 4.5 13.2 0.4
N A:CYS85 4.6 10.6 1.0
CB A:TYR96 4.6 10.0 1.0
O A:HOH1312 4.6 31.7 1.0
HA A:GLU84 4.7 10.8 0.4
HA A:GLU84 4.7 11.1 0.6
N A:ASP97 4.8 9.4 1.0
CA A:GLU84 4.8 11.0 0.4
CA A:GLU84 4.8 11.3 0.6
CD A:PRO86 4.9 10.3 1.0
O A:HOH1396 4.9 40.4 1.0
O A:ALA95 4.9 11.7 1.0
CB A:CYS85 4.9 11.5 0.9
CA A:ASP97 5.0 9.9 1.0
CA A:ALA95 5.0 11.1 1.0
O A:HOH1355 5.0 28.5 1.0
CB A:CYS85 5.0 10.7 0.1

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 04:29:48 2025

Last articles

Mn in 4Q3U
Mn in 4Q3V
Mn in 4Q3T
Mn in 4Q3S
Mn in 4Q3Q
Mn in 4Q3R
Mn in 4Q3P
Mn in 4PXE
Mn in 4PTH
Mn in 4Q0B
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy