Potassium in PDB 2as4: Cytochrome C Peroxidase in Complex with 3-Fluorocatechol

All present enzymatic activity of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol:
1.11.1.5;

The structure of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4 was solved by R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.240, 75.490, 107.040, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / 17.5

The structure of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol also contains other interesting chemical elements:

Fluorine	(F)	2 atoms
Iron	(Fe)	1 atom

The binding sites of Potassium atom in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol (pdb code 2as4). 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 Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4:

Potassium binding site 1 out of 1 in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol within 5.0Å range: probe atom residue distance (Å) B Occ A:K600 b:20.6 occ:0.23 C5 A:3FA500 1.4 30.2 0.8 C3 A:3FA500 1.5 30.3 0.8 F1 A:3FA500 1.9 46.2 0.8 C6 A:3FA500 2.5 26.0 0.8 C1 A:3FA500 2.6 25.4 0.8 O A:HOH1004 2.6 26.0 0.2 O A:LEU177 2.9 16.7 1.0 O A:HIS175 3.0 18.9 1.0 O A:HOH1000 3.0 30.8 0.8 O A:HOH1003 3.1 25.7 0.2 C4 A:3FA500 3.3 26.0 0.8 C2 A:3FA500 3.3 25.4 0.8 O1 A:3FA500 3.6 32.4 0.8 O A:GLY178 3.8 18.3 1.0 C A:GLY178 3.8 15.1 1.0 C A:HIS175 3.8 14.2 1.0 N A:LYS179 3.8 17.3 1.0 O A:HOH1002 3.9 20.1 0.2 C A:LEU177 3.9 15.2 1.0 CA A:LYS179 3.9 17.4 1.0 CA A:HIS175 4.1 14.4 1.0 O A:HOH1001 4.2 15.4 0.2 C A:LYS179 4.3 17.3 1.0 CAD A:HEM400 4.5 14.8 1.0 N A:GLY191 4.5 28.4 1.0 CB A:HIS175 4.5 14.8 1.0 N A:LEU177 4.5 15.4 1.0 O A:HOH1561 4.5 43.8 1.0 CA A:GLY178 4.6 16.0 1.0 O2 A:3FA500 4.6 35.9 0.8 N A:THR180 4.6 17.8 1.0 N A:GLY178 4.6 15.8 1.0 O A:HOH1000 4.7 15.9 0.2 CG A:HIS175 4.7 14.2 1.0 CD2 A:HIS175 4.8 15.5 1.0 O A:LYS179 4.8 19.0 1.0 C3D A:HEM400 4.8 14.0 1.0 C A:ALA176 4.8 16.8 1.0 CA A:LEU177 4.8 15.0 1.0 N A:ALA176 4.9 14.7 1.0 CHA A:HEM400 5.0 15.4 1.0

R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet. Probing Molecular Docking in A Charged Model Binding Site. J.Mol.Biol. V. 357 1449 2006.
ISSN: ISSN 0022-2836
PubMed: 16490206
DOI: 10.1016/J.JMB.2006.01.034