Bromine in PDB 1h3b: Squalene-Hopene Cyclase

All present enzymatic activity of Squalene-Hopene Cyclase:
5.4.99.17;

The structure of Squalene-Hopene Cyclase, PDB code: 1h3b 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 (°)	140.663, 140.663, 243.121, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 25

The binding sites of Bromine atom in the Squalene-Hopene Cyclase (pdb code 1h3b). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Squalene-Hopene Cyclase, PDB code: 1h3b:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Squalene-Hopene Cyclase


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Squalene-Hopene Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ A:Br800 b:94.0 occ:1.00 BR28 A:R46800 0.0 94.0 1.0 C6D A:R46800 1.8 94.0 1.0 C5D A:R46800 2.8 94.0 1.0 C7D A:R46800 2.8 94.0 1.0 NH1 A:ARG127 3.4 37.3 1.0 CD2 A:PHE129 3.5 37.4 1.0 CE1 A:PHE437 3.6 70.8 1.0 O A:HOH2006 3.7 41.9 1.0 CD1 A:PHE437 3.7 70.8 1.0 CE2 A:PHE129 3.8 37.4 1.0 CZ A:PHE437 3.8 70.8 1.0 O A:HOH2023 4.0 35.6 1.0 CG A:PHE437 4.0 70.8 1.0 CE2 A:PHE437 4.0 70.8 1.0 CZ A:ARG127 4.0 37.3 1.0 CD2 A:PHE437 4.1 70.8 1.0 C4D A:R46800 4.1 94.0 1.0 C7P A:R46800 4.1 94.0 1.0 NH2 A:ARG127 4.4 37.3 1.0 CG A:PHE129 4.5 37.4 1.0 O A:HOH2004 4.5 24.6 1.0 C3P A:R46800 4.6 94.0 1.0 NE A:ARG127 4.7 37.3 1.0 CB A:PHE437 4.8 70.8 1.0 CZ A:PHE129 4.9 37.4 1.0 CB A:PHE129 4.9 37.4 1.0

Bromine binding site 2 out of 3 in the Squalene-Hopene Cyclase


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Squalene-Hopene Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ B:Br800 b:82.5 occ:1.00 BR28 B:R46800 0.0 82.5 1.0 C6D B:R46800 1.8 82.5 1.0 C7D B:R46800 2.8 82.5 1.0 C5D B:R46800 2.8 82.5 1.0 CD2 B:PHE129 3.5 36.4 1.0 NH1 B:ARG127 3.5 38.0 1.0 CE1 B:PHE437 3.6 59.4 1.0 CD1 B:PHE437 3.7 59.4 1.0 CE2 B:PHE129 3.8 36.4 1.0 CZ B:PHE437 3.8 59.4 1.0 O B:HOH2008 3.9 37.9 1.0 O B:HOH2031 3.9 25.6 1.0 CG B:PHE437 4.0 59.4 1.0 C7P B:R46800 4.1 82.5 1.0 C4D B:R46800 4.1 82.5 1.0 CE2 B:PHE437 4.1 59.4 1.0 CZ B:ARG127 4.1 38.0 1.0 CD2 B:PHE437 4.2 59.4 1.0 NH2 B:ARG127 4.5 38.0 1.0 CG B:PHE129 4.5 36.4 1.0 C3P B:R46800 4.6 82.5 1.0 O B:HOH2006 4.6 22.5 1.0 CB B:PHE437 4.8 59.4 1.0 NE B:ARG127 4.8 38.0 1.0 CZ B:PHE129 4.9 36.4 1.0

Bromine binding site 3 out of 3 in the Squalene-Hopene Cyclase


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Squalene-Hopene Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ C:Br800 b:95.4 occ:1.00 BR28 C:R46800 0.0 95.4 1.0 C6D C:R46800 1.8 95.4 1.0 C7D C:R46800 2.8 95.4 1.0 C5D C:R46800 2.8 95.4 1.0 CD2 C:PHE129 3.4 29.9 1.0 NH1 C:ARG127 3.5 37.1 1.0 CE1 C:PHE437 3.7 51.7 1.0 O C:HOH2006 3.7 30.4 1.0 CD1 C:PHE437 3.7 51.7 1.0 CE2 C:PHE129 3.7 29.9 1.0 CZ C:PHE437 3.8 51.7 1.0 O C:HOH2033 3.9 29.0 1.0 CG C:PHE437 4.0 51.7 1.0 CZ C:ARG127 4.0 37.1 1.0 O C:HOH2008 4.1 41.8 1.0 CE2 C:PHE437 4.1 51.7 1.0 C7P C:R46800 4.1 95.4 1.0 C4D C:R46800 4.1 95.4 1.0 CD2 C:PHE437 4.1 51.7 1.0 CG C:PHE129 4.4 29.9 1.0 NH2 C:ARG127 4.4 37.1 1.0 C3P C:R46800 4.6 95.4 1.0 NE C:ARG127 4.7 37.1 1.0 CB C:PHE437 4.8 51.7 1.0 CZ C:PHE129 4.8 29.9 1.0 CB C:PHE129 4.9 29.9 1.0 O C:HOH2003 4.9 24.3 1.0 CD C:ARG127 5.0 37.1 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