Fluorine in PDB 4a6l: Beta-Tryptase Inhibitor

All present enzymatic activity of Beta-Tryptase Inhibitor:
3.4.21.59;

The structure of Beta-Tryptase Inhibitor, PDB code: 4a6l was solved by M.Mathieu, S.Maignan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.01 / 2.05
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	82.234, 82.234, 170.654, 90.00, 90.00, 90.00
R / Rfree (%)	18.84 / 21.13

The binding sites of Fluorine atom in the Beta-Tryptase Inhibitor (pdb code 4a6l). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Beta-Tryptase Inhibitor, PDB code: 4a6l:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Beta-Tryptase Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Beta-Tryptase Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F1263 b:39.1 occ:1.00 F30 A:P431263 0.0 39.1 1.0 C29 A:P431263 1.4 37.7 1.0 C28 A:P431263 2.5 36.3 1.0 C24 A:P431263 2.5 38.5 1.0 C23 A:P431263 2.8 41.1 1.0 CD2 C:TYR102 3.4 34.7 1.0 C1 A:P431263 3.5 42.9 1.0 CH2 A:TRP233 3.7 25.9 1.0 CZ3 A:TRP233 3.7 25.5 1.0 C27 A:P431263 3.8 37.3 1.0 CB C:TYR102 3.8 26.9 1.0 C25 A:P431263 3.9 37.3 1.0 CG2 A:ILE193 4.0 29.9 1.0 CG C:TYR102 4.1 31.5 1.0 O C:TYR102 4.2 20.4 1.0 CE2 C:TYR102 4.4 37.6 1.0 CG2 C:THR103 4.4 26.9 1.0 C26 A:P431263 4.4 35.8 1.0 CG A:GLN105 4.6 22.6 1.0 C C:TYR102 4.6 23.9 1.0 C20 A:P431263 4.6 45.2 1.0 CG C:PRO63 4.7 23.7 1.0 CA C:TYR102 4.7 22.8 1.0 CZ2 A:TRP233 4.9 24.7 1.0 CE3 A:TRP233 5.0 23.8 1.0

Fluorine binding site 2 out of 4 in the Beta-Tryptase Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Beta-Tryptase Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:F1263 b:40.8 occ:1.00 F30 B:P431263 0.0 40.8 1.0 C29 B:P431263 1.4 40.8 1.0 C28 B:P431263 2.5 37.7 1.0 C24 B:P431263 2.5 43.0 1.0 C23 B:P431263 2.9 43.3 1.0 CD2 D:TYR102 3.3 31.1 1.0 C1 B:P431263 3.6 42.1 1.0 CH2 B:TRP233 3.7 20.2 1.0 CZ3 B:TRP233 3.7 19.9 1.0 C27 B:P431263 3.8 38.9 1.0 CB D:TYR102 3.9 23.9 1.0 C25 B:P431263 3.9 41.9 1.0 CG2 D:THR103 3.9 27.7 1.0 CG2 B:ILE193 4.0 26.2 1.0 CG D:TYR102 4.0 29.3 1.0 O D:TYR102 4.1 21.7 1.0 CE2 D:TYR102 4.2 32.5 1.0 CG B:GLN105 4.3 24.4 1.0 O D:HOH2045 4.4 40.4 1.0 C26 B:P431263 4.4 40.4 1.0 C D:TYR102 4.5 22.6 1.0 C20 B:P431263 4.7 41.3 1.0 CA D:TYR102 4.7 21.3 1.0 CG D:PRO63 4.8 27.1 1.0 CZ2 B:TRP233 4.9 19.7 1.0 CB B:GLN105 5.0 24.1 1.0 CE3 B:TRP233 5.0 18.5 1.0

Fluorine binding site 3 out of 4 in the Beta-Tryptase Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Beta-Tryptase Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:F1263 b:32.4 occ:1.00 F30 C:P431263 0.0 32.4 1.0 C29 C:P431263 1.4 36.3 1.0 C28 C:P431263 2.5 38.2 1.0 C24 C:P431263 2.5 39.9 1.0 C23 C:P431263 2.9 45.3 1.0 CD2 A:TYR102 3.3 31.4 1.0 C1 C:P431263 3.6 44.0 1.0 CH2 C:TRP233 3.6 22.6 1.0 CZ3 C:TRP233 3.7 22.3 1.0 CB A:TYR102 3.8 25.9 1.0 C25 C:P431263 3.8 38.4 1.0 C27 C:P431263 3.8 38.0 1.0 CG A:TYR102 4.0 29.0 1.0 CG2 C:ILE193 4.0 28.8 1.0 O A:TYR102 4.1 25.8 1.0 CE2 A:TYR102 4.3 31.8 1.0 CG2 A:THR103 4.3 22.3 1.0 C26 C:P431263 4.4 38.9 1.0 C A:TYR102 4.5 25.0 1.0 CG C:GLN105 4.5 23.7 1.0 CA A:TYR102 4.7 23.1 1.0 CG A:PRO63 4.7 28.8 1.0 C20 C:P431263 4.7 43.1 1.0 CZ2 C:TRP233 4.9 21.5 1.0 CE3 C:TRP233 5.0 20.4 1.0

Fluorine binding site 4 out of 4 in the Beta-Tryptase Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Beta-Tryptase Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ D:F1263 b:42.9 occ:1.00 F30 D:P431263 0.0 42.9 1.0 C29 D:P431263 1.4 41.1 1.0 C28 D:P431263 2.4 38.9 1.0 C24 D:P431263 2.5 41.6 1.0 C23 D:P431263 2.9 41.6 1.0 CD2 B:TYR102 3.2 29.9 1.0 C1 D:P431263 3.7 41.9 1.0 CH2 D:TRP233 3.7 22.6 1.0 C27 D:P431263 3.8 40.7 1.0 CB B:TYR102 3.8 24.8 1.0 CZ3 D:TRP233 3.8 21.8 1.0 C25 D:P431263 3.9 38.1 1.0 CG B:TYR102 4.0 27.6 1.0 CG2 B:THR103 4.0 28.4 1.0 CG2 D:ILE193 4.1 25.0 1.0 O B:TYR102 4.1 21.6 1.0 CE2 B:TYR102 4.2 32.0 1.0 C26 D:P431263 4.4 40.2 1.0 CG D:GLN105 4.4 34.7 1.0 C B:TYR102 4.4 22.6 1.0 CA B:TYR102 4.7 21.1 1.0 C20 D:P431263 4.8 45.0 1.0 CG B:PRO63 4.8 30.8 1.0 CZ2 D:TRP233 4.9 22.0 1.0

G.Liang, S.Aldous, G.Merriman, J.Levell, J.Pribish, J.Cairns, X.Chen, S.Maignan, M.Mathieu, J.Tsay, K.Sides, S.Rebello, B.Whitely, I.Morize, H.W.Pauls. Structure-Based Library Design and the Discovery of A Potent and Selective Mast Cell Beta-Tryptase Inhibitor As An Oral Therapeutic Agent. Bioorg.Med.Chem.Lett. V. 22 1049 2012.
ISSN: ISSN 0960-894X
PubMed: 22192588
DOI: 10.1016/J.BMCL.2011.11.119