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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2as4:

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

Fluorine Binding Sites:

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 2as4

Go back to Fluorine Binding Sites List in 2as4
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 2as4

Go back to Fluorine Binding Sites List in 2as4
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

Reference:

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
Page generated: Sun Dec 13 11:34:51 2020

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