Fluorine in PDB 7qm8: Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K

All present enzymatic activity of Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K:
3.4.23.22;

The structure of Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K, PDB code: 7qm8 was solved by C.Y.Huang, S.Aumonier, M.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.33 / 1.79
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.96, 74.323, 53.754, 90, 110.09, 90
R / Rfree (%)	14.2 / 17.2

The binding sites of Fluorine atom in the Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K (pdb code 7qm8). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K, PDB code: 7qm8:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F2804 b:49.8 occ:0.72 F08 A:U1H2804 0.0 49.8 0.7 C07 A:U1H2804 1.4 46.2 0.7 F09 A:U1H2804 2.2 52.1 0.7 F10 A:U1H2804 2.2 48.0 0.7 C06 A:U1H2804 2.4 36.9 0.7 C05 A:U1H2804 3.1 37.5 0.7 C11 A:U1H2804 3.3 38.4 0.7 OD2 A:ASP119 3.5 51.7 1.0 C1 A:DMS2802 3.8 37.3 0.7 C2 A:DMS2802 4.2 51.3 0.7 C04 A:U1H2804 4.4 32.4 0.7 C12 A:U1H2804 4.5 34.6 0.7 S A:DMS2802 4.6 50.2 0.7 CG A:ASP119 4.6 50.8 1.0 OD2 A:ASP81 4.8 56.8 1.0 C03 A:U1H2804 4.9 34.1 0.7

Fluorine binding site 2 out of 3 in the Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F2804 b:52.1 occ:0.72 F09 A:U1H2804 0.0 52.1 0.7 C07 A:U1H2804 1.4 46.2 0.7 F08 A:U1H2804 2.2 49.8 0.7 F10 A:U1H2804 2.2 48.0 0.7 C06 A:U1H2804 2.4 36.9 0.7 C11 A:U1H2804 2.8 38.4 0.7 OG A:SER115 3.6 45.7 1.0 CE1 A:PHE116 3.6 34.8 1.0 C05 A:U1H2804 3.6 37.5 0.7 CD1 A:PHE116 3.7 29.9 1.0 OG A:SER83 3.7 57.7 1.0 CB A:SER115 3.9 37.2 1.0 O A:SER115 3.9 34.0 1.0 C A:SER115 4.0 35.9 1.0 OD2 A:ASP119 4.0 51.7 1.0 C12 A:U1H2804 4.1 34.6 0.7 CZ A:PHE116 4.2 32.8 1.0 N A:PHE116 4.3 28.8 1.0 OD2 A:ASP81 4.3 56.8 1.0 CG A:PHE116 4.4 28.7 1.0 CA A:SER115 4.6 32.5 1.0 CA A:PHE116 4.6 26.4 1.0 CB A:SER83 4.6 40.4 1.0 C04 A:U1H2804 4.8 32.4 0.7 CE2 A:PHE116 4.8 34.3 1.0 CD2 A:PHE116 4.9 32.6 1.0 C03 A:U1H2804 5.0 34.1 0.7

Fluorine binding site 3 out of 3 in the Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Endothiapepsin in Complex with Compound TL00150 in 40% Dmso at 298 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F2804 b:48.0 occ:0.72 F10 A:U1H2804 0.0 48.0 0.7 C07 A:U1H2804 1.4 46.2 0.7 F09 A:U1H2804 2.2 52.1 0.7 F08 A:U1H2804 2.2 49.8 0.7 C06 A:U1H2804 2.4 36.9 0.7 C05 A:U1H2804 2.8 37.5 0.7 OD2 A:ASP119 3.4 51.7 1.0 C11 A:U1H2804 3.6 38.4 0.7 CE1 A:PHE116 3.7 34.8 1.0 CD1 A:PHE116 3.8 29.9 1.0 CD1 A:ILE122 3.8 24.1 1.0 CG A:ASP119 4.1 50.8 1.0 C04 A:U1H2804 4.1 32.4 0.7 CB A:ASP119 4.4 34.7 1.0 O A:SER115 4.6 34.0 1.0 C12 A:U1H2804 4.7 34.6 0.7 O A:HOH3007 4.7 28.4 1.0 CZ A:PHE116 4.8 32.8 1.0 CG A:PHE116 4.9 28.7 1.0 C03 A:U1H2804 4.9 34.1 0.7 OD1 A:ASP119 5.0 59.2 1.0 CG2 A:ILE122 5.0 19.0 1.0

C.Y.Huang, S.Aumonier, S.Engilberge, D.Eris, K.M.L.Smith, F.Leonarski, J.A.Wojdyla, J.H.Beale, D.Buntschu, A.Pauluhn, M.E.Sharpe, A.Metz, V.Olieric, M.Wang. Probing Ligand Binding of Endothiapepsin By `Temperature-Resolved' Macromolecular Crystallography. Acta Crystallogr D Struct V. 78 964 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 35916221
DOI: 10.1107/S205979832200612X