Fluorine 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:

Potassium	(K)	1 atom
Iron	(Fe)	1 atom

The binding sites of Fluorine 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 Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F 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:F500 b:46.2 occ:0.77 F1 A:3FA500 0.0 46.2 0.8 C3 A:3FA500 1.3 30.3 0.8 O A:HOH1004 1.4 26.0 0.2 K A:K600 1.9 20.6 0.2 C1 A:3FA500 2.4 25.4 0.8 C5 A:3FA500 2.4 30.2 0.8 O A:HOH1000 2.7 30.8 0.8 O1 A:3FA500 2.7 32.4 0.8 CA A:LYS179 3.0 17.4 1.0 N A:GLY191 3.1 28.4 1.0 O A:GLY178 3.2 18.3 1.0 CA A:PRO190 3.2 23.0 1.0 C A:PRO190 3.4 26.1 1.0 O A:GLY189 3.4 22.5 1.0 N A:LYS179 3.6 17.3 1.0 C A:GLY178 3.6 15.1 1.0 C2 A:3FA500 3.6 25.4 0.8 C6 A:3FA500 3.6 26.0 0.8 C A:LYS179 3.7 17.3 1.0 N A:THR180 3.8 17.8 1.0 O A:HOH1001 4.0 15.4 0.2 O A:HIS175 4.1 18.9 1.0 CB A:LYS179 4.1 19.8 1.0 CA A:GLY191 4.1 29.6 1.0 O A:LEU177 4.1 16.7 1.0 C4 A:3FA500 4.1 26.0 0.8 N A:PRO190 4.2 24.6 1.0 O A:HOH1003 4.2 25.7 0.2 C A:GLY189 4.2 22.2 1.0 CB A:PRO190 4.2 24.7 1.0 O A:HOH1000 4.3 15.9 0.2 O A:PRO190 4.4 28.6 1.0 O A:HOH1002 4.5 20.1 0.2 O A:LYS179 4.6 19.0 1.0 O2 A:3FA500 4.7 35.9 0.8 CG2 A:THR180 4.7 20.2 1.0 O A:HOH1561 4.8 43.8 1.0 C A:LEU177 4.8 15.2 1.0 CA A:GLY178 4.9 16.0 1.0 SD A:MET230 4.9 21.6 1.0

Fluorine binding site 2 out of 2 in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol within 5.0Å range: probe atom residue distance (Å) B Occ A:F700 b:39.7 occ:1.00 F1 A:3FA700 0.0 39.7 1.0 C3 A:3FA700 1.4 30.8 1.0 C1 A:3FA700 2.4 37.5 1.0 C5 A:3FA700 2.4 30.3 1.0 O1 A:3FA700 2.7 40.9 1.0 OG A:SER104 3.2 24.0 1.0 CE1 A:PHE108 3.4 24.3 1.0 CA A:SER104 3.4 16.0 1.0 CB A:SER104 3.4 18.3 1.0 CZ A:PHE108 3.4 23.3 1.0 C2 A:3FA700 3.6 33.7 1.0 C6 A:3FA700 3.6 30.3 1.0 CD2 A:LEU107 3.7 18.9 1.0 O A:SER104 3.9 15.5 1.0 CD1 A:PHE108 4.0 19.8 1.0 CE2 A:PHE108 4.1 20.6 1.0 C4 A:3FA700 4.1 35.6 1.0 CB A:LEU107 4.1 14.7 1.0 C A:SER104 4.1 15.2 1.0 CG A:LEU107 4.3 14.7 1.0 N A:SER104 4.6 16.7 1.0 CG A:PHE108 4.6 15.6 1.0 CD2 A:PHE108 4.6 17.7 1.0 ND1 A:HIS96 4.6 33.1 1.0 O2 A:3FA700 4.7 37.0 1.0 CG A:HIS96 4.8 27.7 1.0 CE1 A:PHE89 4.9 26.3 1.0 CB A:HIS96 4.9 21.1 1.0 O A:SER103 4.9 15.7 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