Fluorine in PDB 1oq5: Carbonic Anhydrase II in Complex with Nanomolar Inhibitor

All present enzymatic activity of Carbonic Anhydrase II in Complex with Nanomolar Inhibitor:
4.2.1.1;

The structure of Carbonic Anhydrase II in Complex with Nanomolar Inhibitor, PDB code: 1oq5 was solved by A.Weber, A.Casini, A.Heine, D.Kuhn, C.T.Supuran, A.Scozzafava, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.010, 41.070, 71.930, 90.00, 104.20, 90.00
R / Rfree (%)	12.4 / 18.9

The structure of Carbonic Anhydrase II in Complex with Nanomolar Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Carbonic Anhydrase II in Complex with Nanomolar Inhibitor (pdb code 1oq5). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Carbonic Anhydrase II in Complex with Nanomolar Inhibitor, PDB code: 1oq5:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Carbonic Anhydrase II in Complex with Nanomolar Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Carbonic Anhydrase II in Complex with Nanomolar Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:28.5 occ:1.00 F3 A:CEL701 0.0 28.5 1.0 C4 A:CEL701 1.3 25.8 1.0 F1 A:CEL701 2.1 27.7 1.0 F2 A:CEL701 2.1 26.4 1.0 C1 A:CEL701 2.4 22.6 1.0 C2 A:CEL701 3.2 21.8 1.0 CD A:PRO202 3.2 16.0 1.0 N1 A:CEL701 3.3 20.7 1.0 CG A:PRO202 3.3 17.7 1.0 N2 A:CEL701 4.3 20.6 1.0 C3 A:CEL701 4.3 24.3 1.0 CB A:PRO202 4.7 16.7 1.0 N A:PRO202 4.7 16.8 1.0

Fluorine binding site 2 out of 3 in the Carbonic Anhydrase II in Complex with Nanomolar Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Carbonic Anhydrase II in Complex with Nanomolar Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:26.4 occ:1.00 F2 A:CEL701 0.0 26.4 1.0 C4 A:CEL701 1.3 25.8 1.0 F1 A:CEL701 2.1 27.7 1.0 F3 A:CEL701 2.1 28.5 1.0 C1 A:CEL701 2.4 22.6 1.0 N1 A:CEL701 2.7 20.7 1.0 CG A:PRO202 3.3 17.7 1.0 CD1 A:LEU198 3.4 16.6 1.0 CD A:PRO202 3.5 16.0 1.0 C2 A:CEL701 3.7 21.8 1.0 CD1 A:LEU204 3.8 18.8 1.0 CG2 A:VAL135 3.9 18.2 1.0 CG1 A:VAL135 4.0 19.6 1.0 N2 A:CEL701 4.0 20.6 1.0 CB A:VAL135 4.1 17.2 1.0 C3 A:CEL701 4.5 24.3 1.0 CG A:LEU204 4.7 15.9 1.0 CB A:PRO202 4.7 16.7 1.0 CG A:LEU198 4.8 15.2 1.0 CE2 A:PHE131 4.8 17.9 1.0 N A:PRO202 4.9 16.8 1.0 CZ A:PHE131 5.0 16.5 1.0

Fluorine binding site 3 out of 3 in the Carbonic Anhydrase II in Complex with Nanomolar Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Carbonic Anhydrase II in Complex with Nanomolar Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:27.7 occ:1.00 F1 A:CEL701 0.0 27.7 1.0 C4 A:CEL701 1.3 25.8 1.0 F2 A:CEL701 2.1 26.4 1.0 F3 A:CEL701 2.1 28.5 1.0 C1 A:CEL701 2.3 22.6 1.0 C2 A:CEL701 2.9 21.8 1.0 N1 A:CEL701 3.4 20.7 1.0 CE2 A:PHE131 3.6 17.9 1.0 CG2 A:VAL135 3.9 18.2 1.0 C3 A:CEL701 4.1 24.3 1.0 CG1 A:VAL135 4.3 19.6 1.0 N2 A:CEL701 4.3 20.6 1.0 CZ A:PHE131 4.4 16.5 1.0 CD2 A:PHE131 4.4 16.4 1.0 CB A:VAL135 4.6 17.2 1.0 CG A:PRO202 4.9 17.7 1.0 CD A:PRO202 5.0 16.0 1.0 O A:HOH837 5.0 36.4 1.0

A.Weber, A.Casini, A.Heine, D.Kuhn, C.T.Supuran, A.Scozzafava, G.Klebe. Unexpected Nanomolar Inhibition of Carbonic Anhydrase By Cox-2-Selective Celecoxib: New Pharmacological Opportunities Due to Related Binding Site Recognition. J.Med.Chem. V. 47 550 2004.
ISSN: ISSN 0022-2623
PubMed: 14736236
DOI: 10.1021/JM030912M