Chlorine in PDB 1o79: 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: 1o79 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 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	141.289, 141.289, 245.397, 90.00, 90.00, 120.00
R / Rfree (%)	23.9 / 27.3

The binding sites of Chlorine atom in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme (pdb code 1o79). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme, PDB code: 1o79:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl800 b:26.9 occ:1.00 CL31 A:R23800 0.0 26.9 1.0 C4F A:R23800 1.7 26.9 1.0 C5F A:R23800 2.7 26.9 1.0 C3F A:R23800 2.8 26.9 1.0 CB A:ALA170 3.6 6.0 1.0 CA A:ALA170 4.0 13.1 1.0 C6F A:R23800 4.1 26.9 1.0 C2F A:R23800 4.1 26.9 1.0 CE2 A:PHE434 4.2 26.1 1.0 O A:HOH2062 4.3 6.0 1.0 O A:HOH2060 4.4 6.0 1.0 CG2 A:VAL440 4.5 7.2 1.0 CZ A:PHE129 4.5 6.0 1.0 CG1 A:VAL440 4.5 7.2 1.0 C1F A:R23800 4.6 26.9 1.0 O A:ALA170 4.6 13.1 1.0 SG A:CYS435 4.6 44.7 1.0 CD2 A:PHE434 4.7 26.1 1.0 C A:ALA170 4.8 13.1 1.0 CE2 A:PHE129 5.0 6.0 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl800 b:6.3 occ:1.00 CL31 B:R23800 0.0 6.3 1.0 C4F B:R23800 1.8 6.3 1.0 C5F B:R23800 2.8 6.3 1.0 C3F B:R23800 2.8 6.3 1.0 CB B:ALA170 3.5 6.0 1.0 CA B:ALA170 3.8 6.0 1.0 CE2 B:PHE434 4.1 21.0 1.0 C6F B:R23800 4.1 6.3 1.0 C2F B:R23800 4.1 6.3 1.0 O B:ALA170 4.4 6.0 1.0 O B:HOH2062 4.4 6.0 1.0 CZ B:PHE129 4.4 6.0 1.0 C B:ALA170 4.6 6.0 1.0 C1F B:R23800 4.6 6.3 1.0 CG1 B:VAL440 4.7 18.8 1.0 CD2 B:PHE434 4.7 21.0 1.0 CG2 B:VAL440 4.8 18.8 1.0 SG B:CYS435 4.9 19.2 1.0 CG2 B:VAL174 4.9 6.0 1.0 CB B:THR173 5.0 6.0 1.0 CE2 B:PHE129 5.0 6.0 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl800 b:13.7 occ:1.00 CL31 C:R23800 0.0 13.7 1.0 C4F C:R23800 1.8 13.7 1.0 C5F C:R23800 2.7 13.7 1.0 C3F C:R23800 2.8 13.7 1.0 CB C:ALA170 3.5 6.0 1.0 CA C:ALA170 3.8 6.0 1.0 C6F C:R23800 4.1 13.7 1.0 C2F C:R23800 4.1 13.7 1.0 O C:HOH2060 4.1 8.4 1.0 CE2 C:PHE434 4.1 24.9 1.0 O C:ALA170 4.4 6.0 1.0 CZ C:PHE129 4.4 6.0 1.0 C C:ALA170 4.6 6.0 1.0 C1F C:R23800 4.6 13.7 1.0 CG1 C:VAL440 4.7 6.0 1.0 CD2 C:PHE434 4.7 24.9 1.0 CG2 C:VAL440 4.7 6.0 1.0 SG C:CYS435 4.8 21.0 1.0 CG2 C:VAL174 4.9 6.0 1.0 CB C:THR173 4.9 7.3 1.0 CE2 C:PHE129 5.0 6.0 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