Fluorine in PDB 1h3a: Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme

All present enzymatic activity of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme:
5.4.99.17;

The structure of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme, PDB code: 1h3a was solved by A.Lenhart, D.J.Reinert, W.A.Weihofen, J.D.Aebi, H.Dehmlow, O.H.Morand, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	140.904, 140.904, 243.832, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 27

The structure of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme also contains other interesting chemical elements:

Bromine

(Br)

3 atoms

The binding sites of Fluorine atom in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme (pdb code 1h3a). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme, PDB code: 1h3a:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:F800 b:30.6 occ:1.00 F A:R04800 0.0 30.6 1.0 C5C A:R04800 1.3 30.6 1.0 C4C A:R04800 2.4 30.6 1.0 C6C A:R04800 2.4 30.6 1.0 O A:R04800 2.8 55.6 1.0 CD1 A:LEU607 3.3 9.6 1.0 CD2 A:LEU36 3.3 8.6 1.0 CB A:SER307 3.4 7.4 1.0 CD2 A:LEU607 3.7 9.6 1.0 C3P A:R04800 3.7 30.6 1.0 C7C A:R04800 3.7 30.6 1.0 CB A:ALA306 3.9 17.8 1.0 CG A:LEU607 4.1 9.6 1.0 N A:SER307 4.1 22.3 1.0 C7P A:R04800 4.2 30.6 1.0 C A:ALA306 4.2 12.0 1.0 C4B A:R04800 4.2 55.6 1.0 O A:ALA306 4.4 12.0 1.0 CA A:SER307 4.4 22.3 1.0 OG A:SER307 4.4 7.4 1.0 CG A:LEU36 4.4 8.6 1.0 CE2 A:PHE605 4.5 16.2 1.0 CA A:ALA306 4.7 12.0 1.0 C3B A:R04800 5.0 55.6 1.0

Fluorine binding site 2 out of 3 in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:F800 b:28.4 occ:1.00 F B:R04800 0.0 28.4 1.0 C5C B:R04800 1.3 28.4 1.0 C4C B:R04800 2.4 28.4 1.0 C6C B:R04800 2.4 28.4 1.0 O B:R04800 2.8 31.7 1.0 CD2 B:LEU36 3.3 7.0 1.0 CD1 B:LEU607 3.3 7.0 1.0 CB B:SER307 3.4 7.0 1.0 C3P B:R04800 3.7 28.4 1.0 CD2 B:LEU607 3.7 7.0 1.0 C7C B:R04800 3.7 28.4 1.0 CB B:ALA306 3.8 7.0 1.0 N B:SER307 4.1 20.2 1.0 C B:ALA306 4.1 7.0 1.0 CG B:LEU607 4.1 7.0 1.0 C7P B:R04800 4.2 28.4 1.0 C4B B:R04800 4.2 31.7 1.0 O B:ALA306 4.3 7.0 1.0 CA B:SER307 4.3 20.2 1.0 OG B:SER307 4.4 7.0 1.0 CG B:LEU36 4.4 7.0 1.0 CE2 B:PHE605 4.5 7.9 1.0 CA B:ALA306 4.6 7.0 1.0 C3B B:R04800 5.0 31.7 1.0

Fluorine binding site 3 out of 3 in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:F800 b:32.8 occ:1.00 F C:R04800 0.0 32.8 1.0 C5C C:R04800 1.3 32.8 1.0 C4C C:R04800 2.4 32.8 1.0 C6C C:R04800 2.4 32.8 1.0 O C:R04800 2.8 27.4 1.0 CD1 C:LEU607 3.3 23.7 1.0 CD2 C:LEU36 3.4 12.3 1.0 CB C:SER307 3.4 7.0 1.0 CD2 C:LEU607 3.7 23.7 1.0 C3P C:R04800 3.7 32.8 1.0 C7C C:R04800 3.7 32.8 1.0 CB C:ALA306 3.8 7.0 1.0 CG C:LEU607 4.1 23.7 1.0 C C:ALA306 4.1 14.9 1.0 N C:SER307 4.1 15.2 1.0 C7P C:R04800 4.2 32.8 1.0 C4B C:R04800 4.2 27.4 1.0 O C:ALA306 4.3 14.9 1.0 CA C:SER307 4.4 15.2 1.0 OG C:SER307 4.4 7.0 1.0 CE2 C:PHE605 4.5 14.6 1.0 CG C:LEU36 4.5 12.3 1.0 CA C:ALA306 4.6 14.9 1.0

A.Lenhart, D.J.Reinert, J.D.Aebi, H.Dehmlow, O.H.Morand, G.E.Schulz. Binding Structures and Potencies of Oxidosqualene Cyclase Inhibitors with the Homologous Squalene-Hopene Cyclase J.Med.Chem. V. 46 2083 2003.
ISSN: ISSN 0022-2623
PubMed: 12747780
DOI: 10.1021/JM0211218