Fluorine in PDB 8b75: Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861

All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861:
4.6.1.1;

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861, PDB code: 8b75 was solved by C.Steegborn, M.Kehr, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.94 / 1.82
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	100.131, 100.131, 97.889, 90, 90, 120
R / Rfree (%)	20.3 / 24.6

The structure of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861 (pdb code 8b75). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861, PDB code: 8b75:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:29.2 occ:1.00 FAZ A:PJU501 0.0 29.2 1.0 CAX A:PJU501 1.3 27.6 1.0 FAY A:PJU501 2.2 29.7 1.0 NAT A:PJU501 2.3 24.3 1.0 NAW A:PJU501 2.9 24.3 1.0 C A:PHE96 3.0 21.0 1.0 N A:ALA97 3.1 23.1 1.0 O A:PHE96 3.3 21.9 1.0 O A:LYS95 3.4 21.0 1.0 CB A:ALA97 3.4 26.9 1.0 CAU A:PJU501 3.4 21.2 1.0 CA A:PHE96 3.5 19.5 1.0 C A:LYS95 3.5 20.9 1.0 N A:PHE96 3.6 19.4 1.0 CA A:ALA97 3.8 27.4 1.0 CB A:LYS95 3.8 22.6 1.0 CE1 A:PHE336 3.8 28.5 1.0 O A:ALA100 4.0 27.3 1.0 CAV A:PJU501 4.1 22.8 1.0 CA A:LEU101 4.2 23.1 1.0 CA A:LYS95 4.3 21.4 1.0 CAI A:PJU501 4.3 22.2 1.0 C A:ALA100 4.4 29.2 1.0 CZ A:PHE336 4.6 28.4 1.0 N A:LEU102 4.6 20.8 1.0 CD1 A:PHE336 4.6 27.0 1.0 N A:LEU101 4.7 22.6 1.0 CB A:ALA100 4.8 31.4 1.0 C A:LEU101 4.8 23.2 1.0 CB A:PHE96 4.9 18.8 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human Soluble Adenylyl Cyclase in Complex with the Inhibitor Tdi-011861 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:29.7 occ:1.00 FAY A:PJU501 0.0 29.7 1.0 CAX A:PJU501 1.3 27.6 1.0 FAZ A:PJU501 2.2 29.2 1.0 NAT A:PJU501 2.3 24.3 1.0 CA A:LEU101 3.1 23.1 1.0 CAU A:PJU501 3.1 21.2 1.0 NAW A:PJU501 3.2 24.3 1.0 C A:LEU101 3.2 23.2 1.0 CB A:ALA100 3.3 31.4 1.0 N A:LEU102 3.3 20.8 1.0 N A:LEU101 3.3 22.6 1.0 C A:ALA100 3.4 29.2 1.0 O A:ALA100 3.8 27.3 1.0 O A:LYS95 3.8 21.0 1.0 O A:LEU101 3.8 22.9 1.0 CE2 A:PHE45 3.8 34.6 1.0 CB A:LEU102 3.9 20.1 1.0 CA A:ALA100 4.0 30.8 1.0 CA A:LEU102 4.2 20.6 1.0 CAI A:PJU501 4.2 22.2 1.0 CAV A:PJU501 4.2 22.8 1.0 CD2 A:PHE45 4.3 31.4 1.0 N A:ALA97 4.4 23.1 1.0 CZ A:PHE45 4.5 33.4 1.0 C A:LYS95 4.5 20.9 1.0 CB A:LEU101 4.5 22.8 1.0 CB A:ALA97 4.5 26.9 1.0 C A:PHE96 4.7 21.0 1.0 CA A:PHE96 4.7 19.5 1.0 N A:ALA100 4.9 38.8 1.0 N A:PHE96 5.0 19.4 1.0

M.Miller, T.Rossetti, J.Ferreira, L.Ghanem, M.Balbach, N.Kaur, L.R.Levin, J.Buck, M.Kehr, S.Coquille, J.Van Den Heuvel, C.Steegborn, M.Fushimi, E.Finkin-Groner, R.W.Myers, S.Kargman, N.J.Liverton, D.J.Huggins, P.T.Meinke. Design, Synthesis, and Pharmacological Evaluation of Second-Generation Soluble Adenylyl Cyclase (Sac, ADCY10) Inhibitors with Slow Dissociation Rates. J.Med.Chem. V. 65 15208 2022.
ISSN: ISSN 0022-2623
PubMed: 36346696
DOI: 10.1021/ACS.JMEDCHEM.2C01133