Bromine in PDB 3pi5: Crystal Structure of Human Beta Secretase in Complex with BFG356

All present enzymatic activity of Crystal Structure of Human Beta Secretase in Complex with BFG356:
3.4.23.46;

The structure of Crystal Structure of Human Beta Secretase in Complex with BFG356, PDB code: 3pi5 was solved by J.M.Rondeau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.22 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.486, 102.416, 100.178, 90.00, 104.45, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Bromine atom in the Crystal Structure of Human Beta Secretase in Complex with BFG356 (pdb code 3pi5). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Crystal Structure of Human Beta Secretase in Complex with BFG356, PDB code: 3pi5:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Crystal Structure of Human Beta Secretase in Complex with BFG356


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human Beta Secretase in Complex with BFG356 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br387 b:77.0 occ:1.00 BR1 A:3P5387 0.0 77.0 1.0 C2 A:3P5387 1.9 55.6 1.0 C3 A:3P5387 2.9 53.6 1.0 C9 A:3P5387 2.9 49.9 1.0 O54 A:3P5387 3.1 49.1 1.0 CD1 A:ILE110 3.6 59.0 1.0 O A:GLN12 3.9 53.6 1.0 O A:HOH460 4.1 64.7 1.0 CZ2 A:TRP115 4.1 41.3 1.0 C A:GLN12 4.1 54.3 1.0 C4 A:3P5387 4.2 54.5 1.0 C8 A:3P5387 4.2 48.5 1.0 CD2 A:LEU30 4.4 46.4 1.0 O A:GLY230 4.5 42.8 1.0 N A:GLY13 4.6 51.7 1.0 CA A:GLN12 4.6 56.6 1.0 CG1 A:ILE110 4.6 59.0 1.0 C6 A:3P5387 4.7 48.8 1.0 CA A:GLY13 4.8 48.2 1.0 CD1 A:LEU30 4.9 42.9 1.0 CE2 A:TRP115 4.9 40.9 1.0 CH2 A:TRP115 4.9 40.9 1.0 O A:GLY11 5.0 53.1 1.0

Bromine binding site 2 out of 3 in the Crystal Structure of Human Beta Secretase in Complex with BFG356


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human Beta Secretase in Complex with BFG356 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br387 b:72.9 occ:1.00 BR1 B:3P5387 0.0 72.9 1.0 C2 B:3P5387 1.9 59.7 1.0 C3 B:3P5387 2.9 57.1 1.0 C9 B:3P5387 2.9 52.3 1.0 O54 B:3P5387 3.1 55.3 1.0 CD1 B:ILE110 3.6 59.6 1.0 O B:GLN12 3.9 51.4 1.0 C B:GLN12 4.0 52.8 1.0 CZ2 B:TRP115 4.1 43.1 1.0 O B:HOH406 4.1 60.0 1.0 C4 B:3P5387 4.2 56.3 1.0 C8 B:3P5387 4.2 52.4 1.0 CD2 B:LEU30 4.3 44.1 1.0 N B:GLY13 4.5 52.4 1.0 O B:GLY230 4.5 40.6 1.0 CA B:GLN12 4.5 54.8 1.0 CG1 B:ILE110 4.6 60.1 1.0 C6 B:3P5387 4.7 51.6 1.0 CA B:GLY13 4.7 51.5 1.0 CD1 B:LEU30 4.8 46.3 1.0 CE2 B:TRP115 4.8 39.8 1.0 O B:HOH445 4.9 44.7 1.0 NE1 B:TRP115 4.9 40.3 1.0 CH2 B:TRP115 4.9 42.0 1.0 O B:GLY11 5.0 51.8 1.0

Bromine binding site 3 out of 3 in the Crystal Structure of Human Beta Secretase in Complex with BFG356


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Human Beta Secretase in Complex with BFG356 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br387 b:76.1 occ:1.00 BR1 C:3P5387 0.0 76.1 1.0 C2 C:3P5387 1.9 58.0 1.0 C3 C:3P5387 2.8 55.1 1.0 C9 C:3P5387 2.9 51.6 1.0 O54 C:3P5387 3.1 52.1 1.0 CD1 C:ILE110 3.6 58.1 1.0 O C:GLN12 3.9 55.1 1.0 CZ2 C:TRP115 4.1 44.6 1.0 C C:GLN12 4.1 56.1 1.0 C4 C:3P5387 4.1 52.0 1.0 C8 C:3P5387 4.2 47.5 1.0 CD2 C:LEU30 4.3 44.7 1.0 O C:GLY230 4.5 40.6 1.0 N C:GLY13 4.6 55.0 1.0 CA C:GLN12 4.6 58.4 1.0 CG1 C:ILE110 4.6 57.1 1.0 C6 C:3P5387 4.7 50.5 1.0 CD1 C:LEU30 4.8 42.3 1.0 CA C:GLY13 4.8 54.3 1.0 CE2 C:TRP115 4.8 44.7 1.0 CH2 C:TRP115 4.9 43.7 1.0 NE1 C:TRP115 4.9 44.4 1.0 O C:GLY11 5.0 59.0 1.0

H.Rueeger, J.M.Rondeau, C.Mccarthy, H.Mobitz, M.Tintelnot-Blomley, U.Neumann, S.Desrayaud. Structure Based Design, Synthesis and Sar of Cyclic Hydroxyethylamine (Hea) Bace-1 Inhibitors. Bioorg.Med.Chem.Lett. V. 21 1942 2011.
ISSN: ISSN 0960-894X
PubMed: 21388807
DOI: 10.1016/J.BMCL.2011.02.038