Fluorine in PDB 3ooz: BACE1 in Complex with the Aminohydantoin Compound 102

All present enzymatic activity of BACE1 in Complex with the Aminohydantoin Compound 102:
3.4.23.46;

The structure of BACE1 in Complex with the Aminohydantoin Compound 102, PDB code: 3ooz was solved by A.M.Olland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.70 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.927, 104.664, 50.540, 90.00, 94.91, 90.00
R / Rfree (%)	21.5 / 25.3

The binding sites of Fluorine atom in the BACE1 in Complex with the Aminohydantoin Compound 102 (pdb code 3ooz). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the BACE1 in Complex with the Aminohydantoin Compound 102, PDB code: 3ooz:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the BACE1 in Complex with the Aminohydantoin Compound 102


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of BACE1 in Complex with the Aminohydantoin Compound 102 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:28.0 occ:1.00 F1 A:ZOO1 0.0 28.0 1.0 C11 A:ZOO1 1.3 24.8 1.0 F2 A:ZOO1 2.2 26.3 1.0 O2 A:ZOO1 2.2 23.1 1.0 CG A:ARG190 3.3 23.4 1.0 OD1 A:ASN99 3.3 17.2 1.0 O A:HOH480 3.4 18.9 1.0 C8 A:ZOO1 3.5 20.9 1.0 CZ2 A:TRP138 3.6 25.5 1.0 CB A:ARG190 3.7 21.7 1.0 CG A:ASN99 3.7 17.1 1.0 CG1 A:VAL131 3.8 31.9 1.0 NE1 A:TRP138 3.9 25.3 1.0 CG2 A:VAL131 4.0 31.8 1.0 CE2 A:TRP138 4.1 26.0 1.0 CB A:ASN99 4.1 15.7 1.0 C9 A:ZOO1 4.2 20.5 1.0 CB A:VAL131 4.3 32.5 1.0 C7 A:ZOO1 4.4 20.6 1.0 O A:HOH14 4.5 14.2 1.0 ND2 A:ASN99 4.5 16.4 1.0 N A:ARG190 4.7 21.0 1.0 CH2 A:TRP138 4.7 25.1 1.0 CD A:ARG190 4.7 26.7 1.0 CA A:ARG190 4.8 21.5 1.0

Fluorine binding site 2 out of 4 in the BACE1 in Complex with the Aminohydantoin Compound 102


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of BACE1 in Complex with the Aminohydantoin Compound 102 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:26.3 occ:1.00 F2 A:ZOO1 0.0 26.3 1.0 C11 A:ZOO1 1.4 24.8 1.0 F1 A:ZOO1 2.2 28.0 1.0 O2 A:ZOO1 2.2 23.1 1.0 C8 A:ZOO1 3.0 20.9 1.0 CZ2 A:TRP138 3.0 25.5 1.0 C9 A:ZOO1 3.1 20.5 1.0 O A:HOH14 3.2 14.2 1.0 NE1 A:TRP138 3.2 25.3 1.0 CE2 A:TRP138 3.4 26.0 1.0 CB A:ASN99 3.5 15.7 1.0 CG A:ASN99 4.0 17.1 1.0 OD1 A:ASN99 4.1 17.2 1.0 CB A:ALA101 4.1 15.8 1.0 CH2 A:TRP138 4.2 25.1 1.0 C7 A:ZOO1 4.3 20.6 1.0 O A:HOH480 4.3 18.9 1.0 C10 A:ZOO1 4.5 18.6 1.0 CD1 A:TRP138 4.5 25.8 1.0 CA A:ASN99 4.7 15.1 1.0 CD2 A:TRP138 4.8 25.5 1.0 ND2 A:ASN99 4.8 16.4 1.0 N A:ASN99 4.8 14.8 1.0 O A:ASN99 4.9 15.3 1.0

Fluorine binding site 3 out of 4 in the BACE1 in Complex with the Aminohydantoin Compound 102


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of BACE1 in Complex with the Aminohydantoin Compound 102 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:27.7 occ:1.00 F3 A:ZOO1 0.0 27.7 1.0 C22 A:ZOO1 1.4 25.6 1.0 C21 A:ZOO1 2.3 24.4 1.0 C20 A:ZOO1 2.5 21.7 1.0 O A:HOH556 2.9 37.7 1.0 C19 A:ZOO1 3.2 21.3 1.0 C A:GLY292 3.4 15.5 1.0 O A:SER291 3.4 14.7 1.0 CA A:GLY75 3.4 18.8 1.0 CA A:GLY292 3.5 14.4 1.0 O A:GLY292 3.6 16.5 1.0 O A:HOH489 3.8 29.5 1.0 N A:THR293 3.9 15.0 1.0 O A:HOH19 3.9 16.4 1.0 N A:GLY75 4.0 19.9 1.0 C18 A:ZOO1 4.0 20.5 1.0 CD1 A:LEU92 4.1 15.1 1.0 C A:SER291 4.3 13.9 1.0 N A:GLY292 4.4 14.0 1.0 C A:THR293 4.4 15.1 1.0 CA A:THR293 4.5 15.4 1.0 OG1 A:THR294 4.5 18.5 1.0 N A:THR294 4.5 16.1 1.0 C A:GLN74 4.7 20.6 1.0 CD2 A:LEU92 4.7 13.8 1.0 C A:GLY75 4.7 18.2 1.0 O A:THR293 4.8 13.9 1.0 N A:TYR76 4.9 16.2 1.0 O A:GLN74 5.0 20.8 1.0 CG A:LEU92 5.0 13.0 1.0

Fluorine binding site 4 out of 4 in the BACE1 in Complex with the Aminohydantoin Compound 102


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of BACE1 in Complex with the Aminohydantoin Compound 102 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:20.0 occ:1.00 F4 A:ZOO1 0.0 20.0 1.0 C15 A:ZOO1 1.3 20.6 1.0 C14 A:ZOO1 2.4 21.1 1.0 C16 A:ZOO1 2.4 20.4 1.0 C18 A:ZOO1 2.8 20.5 1.0 O A:HOH546 2.9 26.2 1.0 O A:PHE170 3.0 22.7 1.0 CH2 A:TRP177 3.2 16.9 1.0 CZ2 A:TRP177 3.4 17.1 1.0 CD1 A:ILE172 3.4 22.2 1.0 CG1 A:ILE172 3.5 22.6 1.0 C19 A:ZOO1 3.6 21.3 1.0 C13 A:ZOO1 3.6 20.8 1.0 C17 A:ZOO1 3.7 20.2 1.0 C12 A:ZOO1 4.1 20.0 1.0 C A:PHE170 4.2 23.3 1.0 CZ3 A:TRP177 4.5 16.5 1.0 C20 A:ZOO1 4.8 21.7 1.0 CE2 A:TRP177 4.8 15.3 1.0 CB A:ILE172 4.9 22.5 1.0 CD1 A:ILE180 4.9 16.9 1.0 N A:ILE172 5.0 22.9 1.0

M.S.Malamas, A.Robichaud, J.Erdei, D.Quagliato, W.Solvibile, P.Zhou, K.Morris, J.Turner, E.Wagner, K.Fan, A.Olland, S.Jacobsen, P.Reinhart, D.Riddell, M.Pangalos. Design and Synthesis of Aminohydantoins As Potent and Selective Human Beta-Secretase (BACE1) Inhibitors with Enhanced Brain Permeability Bioorg.Med.Chem.Lett. V. 20 6597 2010.
ISSN: ISSN 0960-894X
PubMed: 20880704
DOI: 10.1016/J.BMCL.2010.09.029