Fluorine in PDB 2eu3: Human Carbonic Anhydrase II in Complex with Novel Inhibitors

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Novel Inhibitors:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with Novel Inhibitors, PDB code: 2eu3 was solved by S.Z.Fisher, L.Govindasamy, N.Boyle, M.Agbandje-Mckenna, D.N.Silverman, G.M.Blackburn, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.278, 41.396, 72.204, 90.00, 103.96, 90.00
R / Rfree (%)	n/a / n/a

The structure of Human Carbonic Anhydrase II in Complex with Novel Inhibitors also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Human Carbonic Anhydrase II in Complex with Novel Inhibitors (pdb code 2eu3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human Carbonic Anhydrase II in Complex with Novel Inhibitors, PDB code: 2eu3:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Carbonic Anhydrase II in Complex with Novel Inhibitors


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Carbonic Anhydrase II in Complex with Novel Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:F263 b:34.4 occ:1.00 F1 A:FF3263 0.0 34.4 1.0 C3 A:FF3263 1.3 17.6 1.0 F2 A:FF3263 2.1 60.1 1.0 C2 A:FF3263 2.4 16.6 1.0 S2 A:FF3263 2.6 14.9 1.0 N2 A:FF3263 2.9 18.7 1.0 O1 A:FF3263 2.9 14.3 1.0 O2 A:FF3263 3.1 16.9 1.0 CD2 A:LEU198 3.3 14.7 1.0 CB A:LEU198 3.8 13.8 1.0 N3 A:FF3263 3.9 9.5 1.0 S1 A:FF3263 4.0 21.4 1.0 CG A:LEU198 4.0 13.2 1.0 N1 A:FF3263 4.1 22.5 1.0 OG1 A:THR200 4.3 21.2 1.0 CA A:LEU198 4.4 8.6 1.0 CD1 A:LEU198 4.4 18.2 1.0 C1 A:FF3263 4.7 23.4 1.0 N A:THR199 4.8 10.5 1.0 CE1 A:HIS94 4.9 11.4 1.0

Fluorine binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with Novel Inhibitors


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Carbonic Anhydrase II in Complex with Novel Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:F263 b:60.1 occ:1.00 F2 A:FF3263 0.0 60.1 1.0 C3 A:FF3263 1.3 17.6 1.0 F1 A:FF3263 2.1 34.4 1.0 C2 A:FF3263 2.4 16.6 1.0 OG1 A:THR200 2.5 21.2 1.0 S2 A:FF3263 2.6 14.9 1.0 O1 A:FF3263 2.8 14.3 1.0 N3 A:FF3263 3.1 9.5 1.0 S1 A:FF3263 3.2 21.4 1.0 N A:THR200 3.3 12.2 1.0 N A:THR199 3.5 10.5 1.0 CB A:THR200 3.5 14.0 1.0 N2 A:FF3263 3.6 18.7 1.0 CB A:LEU198 3.7 13.8 1.0 CG2 A:THR200 3.7 14.8 1.0 O2 A:FF3263 3.8 16.9 1.0 CA A:THR200 3.9 10.6 1.0 CA A:LEU198 4.1 8.6 1.0 C A:THR199 4.2 10.3 1.0 O A:THR200 4.2 15.0 1.0 C A:LEU198 4.2 12.7 1.0 OG1 A:THR199 4.2 13.3 1.0 CA A:THR199 4.4 11.0 1.0 C1 A:FF3263 4.5 23.4 1.0 CD2 A:LEU198 4.5 14.7 1.0 N1 A:FF3263 4.5 22.5 1.0 C A:THR200 4.5 12.5 1.0 CG A:LEU198 4.6 13.2 1.0 ZN A:ZN262 4.8 10.4 1.0 CD1 A:LEU198 4.9 18.2 1.0 CB A:THR199 4.9 14.2 1.0

S.Z.Fisher, L.Govindasamy, N.Boyle, M.Agbandje-Mckenna, D.N.Silverman, G.M.Blackburn, R.Mckenna. X-Ray Crystallographic Studies Reveal That the Incorporation of Spacer Groups in Carbonic Anhydrase Inhibitors Causes Alternate Binding Modes. Acta Crystallogr.,Sect.F V. 62 618 2006.
ISSN: ESSN 1744-3091
PubMed: 16820676
DOI: 10.1107/S1744309106020446