Atomistry » Bromine » PDB 1m9t-1p1y » 1o6r
Atomistry »
  Bromine »
    PDB 1m9t-1p1y »
      1o6r »

Bromine in PDB 1o6r: Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme

Enzymatic activity of 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;

Protein crystallography data

The structure of Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme, PDB code: 1o6r 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 / 2.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 140.627, 140.627, 244.030, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 23.6

Bromine Binding Sites:

The binding sites of Bromine atom in the Structures of Human Oxidosqualene Cyclase Inhibitors Bound to An Homologous Enzyme (pdb code 1o6r). 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: 1o6r:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in 1o6r

Go back to Bromine Binding Sites List in 1o6r
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:69.9
occ:1.00
BR27 A:R19800 0.0 69.9 1.0
C4D A:R19800 1.9 69.9 1.0
C3D A:R19800 2.9 69.9 1.0
C5D A:R19800 2.9 69.9 1.0
CB A:ALA170 3.9 18.1 1.0
CZ A:PHE129 4.0 24.3 1.0
CA A:ALA170 4.1 26.0 1.0
O A:HOH2054 4.2 20.7 1.0
C2D A:R19800 4.2 69.9 1.0
C6D A:R19800 4.3 69.9 1.0
CG2 A:VAL440 4.3 40.0 1.0
CE2 A:PHE434 4.4 50.9 1.0
CE2 A:PHE129 4.4 24.3 1.0
O A:HOH2053 4.6 17.7 1.0
C1D A:R19800 4.8 69.9 1.0
CB A:THR173 4.8 21.2 1.0
CG2 A:THR173 4.9 21.2 1.0
O A:ALA170 4.9 26.0 1.0
CD2 A:PHE434 5.0 50.9 1.0
C A:ALA170 5.0 26.0 1.0

Bromine binding site 2 out of 3 in 1o6r

Go back to Bromine Binding Sites List in 1o6r
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:62.1
occ:1.00
BR27 B:R19800 0.0 62.1 1.0
C4D B:R19800 1.9 62.1 1.0
C3D B:R19800 2.9 62.1 1.0
C5D B:R19800 2.9 62.1 1.0
CB B:ALA170 3.8 21.9 1.0
CA B:ALA170 4.0 18.8 1.0
CZ B:PHE129 4.0 26.7 1.0
O B:HOH2073 4.1 36.7 1.0
C2D B:R19800 4.2 62.1 1.0
C6D B:R19800 4.2 62.1 1.0
CG2 B:VAL440 4.2 24.7 1.0
CE2 B:PHE434 4.3 33.6 1.0
CE2 B:PHE129 4.5 26.7 1.0
O B:HOH2072 4.7 18.9 1.0
C1D B:R19800 4.8 62.1 1.0
O B:ALA170 4.8 18.8 1.0
CB B:THR173 4.9 20.0 1.0
CG2 B:THR173 4.9 20.0 1.0
C B:ALA170 4.9 18.8 1.0
CD2 B:PHE434 5.0 33.6 1.0
N B:ALA170 5.0 18.8 1.0

Bromine binding site 3 out of 3 in 1o6r

Go back to Bromine Binding Sites List in 1o6r
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:61.2
occ:1.00
BR27 C:R19800 0.0 61.2 1.0
C4D C:R19800 1.9 61.2 1.0
C5D C:R19800 2.9 61.2 1.0
C3D C:R19800 2.9 61.2 1.0
CB C:ALA170 3.7 7.9 1.0
CA C:ALA170 3.9 17.4 1.0
CZ C:PHE129 4.0 12.9 1.0
O C:HOH2063 4.1 28.4 1.0
C6D C:R19800 4.2 61.2 1.0
C2D C:R19800 4.2 61.2 1.0
CG2 C:VAL440 4.2 25.7 1.0
CE2 C:PHE434 4.3 38.0 1.0
CE2 C:PHE129 4.5 12.9 1.0
CB C:THR173 4.7 23.7 1.0
O C:ALA170 4.8 17.4 1.0
C1D C:R19800 4.8 61.2 1.0
CG2 C:THR173 4.8 23.7 1.0
C C:ALA170 4.8 17.4 1.0
N C:ALA170 4.9 17.4 1.0
CD2 C:PHE434 5.0 38.0 1.0
CE1 C:PHE129 5.0 12.9 1.0

Reference:

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
Page generated: Mon Jul 7 03:37:20 2025

Last articles

Br in 5MOW
Br in 5MLJ
Br in 5MAA
Br in 5MFT
Br in 5M91
Br in 5M8U
Br in 5M2G
Br in 5LXY
Br in 5M65
Br in 5M76
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy