Bromine in PDB 1h39: 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: 1h39 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 (°)	140.784, 140.784, 244.033, 90.00, 90.00, 120.00
R / Rfree (%)	22.5 / 25.5

The binding sites of Bromine atom in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme (pdb code 1h39). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme, PDB code: 1h39:
Jump to Bromine binding site number: 1; 2; 3;

Bromine 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 Bromine with other atoms in the Br 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:Br800 b:71.2 occ:1.00 BR27 A:R03800 0.0 71.2 1.0 C4D A:R03800 1.9 71.2 1.0 C5D A:R03800 2.9 71.2 1.0 C3D A:R03800 2.9 71.2 1.0 CB A:ALA170 3.7 51.9 1.0 CE2 A:PHE434 4.1 54.0 1.0 CA A:ALA170 4.1 24.4 1.0 C6D A:R03800 4.2 71.2 1.0 C2D A:R03800 4.2 71.2 1.0 CZ A:PHE129 4.3 46.0 1.0 O A:HOH2059 4.6 23.7 1.0 CD2 A:PHE434 4.6 54.0 1.0 CG1 A:VAL440 4.6 48.7 1.0 SG A:CYS435 4.6 86.6 1.0 O A:ALA170 4.6 24.4 1.0 C1D A:R03800 4.7 71.2 1.0 CG2 A:THR173 4.8 23.5 1.0 CG2 A:VAL440 4.8 48.7 1.0 CB A:THR173 4.8 23.5 1.0 C A:ALA170 4.8 24.4 1.0 CE2 A:PHE129 4.9 46.0 1.0

Bromine 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 Bromine with other atoms in the Br 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:Br800 b:60.7 occ:1.00 BR27 B:R03800 0.0 60.7 1.0 C4D B:R03800 1.9 60.7 1.0 C3D B:R03800 2.9 60.7 1.0 C5D B:R03800 2.9 60.7 1.0 CB B:ALA170 3.6 31.4 1.0 CA B:ALA170 3.9 15.4 1.0 CE2 B:PHE434 4.1 62.7 1.0 C2D B:R03800 4.2 60.7 1.0 C6D B:R03800 4.2 60.7 1.0 CZ B:PHE129 4.4 50.1 1.0 O B:ALA170 4.4 15.4 1.0 C B:ALA170 4.6 15.4 1.0 CG1 B:VAL440 4.6 63.8 1.0 CG2 B:THR173 4.7 17.3 1.0 CB B:THR173 4.7 17.3 1.0 CD2 B:PHE434 4.7 62.7 1.0 SG B:CYS435 4.7 47.9 1.0 C1D B:R03800 4.7 60.7 1.0 CG2 B:VAL174 4.9 20.8 1.0 CG2 B:VAL440 4.9 63.8 1.0 CE2 B:PHE129 5.0 50.1 1.0

Bromine 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 Bromine with other atoms in the Br 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:Br800 b:63.7 occ:1.00 BR27 C:R03800 0.0 63.7 1.0 C4D C:R03800 1.9 63.7 1.0 C3D C:R03800 2.9 63.7 1.0 C5D C:R03800 2.9 63.7 1.0 CB C:ALA170 3.7 31.0 1.0 CA C:ALA170 4.0 24.9 1.0 CE2 C:PHE434 4.0 43.0 1.0 C6D C:R03800 4.2 63.7 1.0 C2D C:R03800 4.2 63.7 1.0 CZ C:PHE129 4.4 34.9 1.0 O C:ALA170 4.5 24.9 1.0 CD2 C:PHE434 4.6 43.0 1.0 CG1 C:VAL440 4.6 48.1 1.0 SG C:CYS435 4.6 53.9 1.0 C C:ALA170 4.7 24.9 1.0 CG2 C:THR173 4.7 34.9 1.0 CB C:THR173 4.7 34.9 1.0 C1D C:R03800 4.7 63.7 1.0 CG2 C:VAL174 4.8 26.9 1.0 CG2 C:VAL440 4.9 48.1 1.0 CE2 C:PHE129 5.0 34.9 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