Fluorine in PDB 7qm7: Endothiapepsin in Complex with Compound TL00150 in 20% Dmso at 298 K

All present enzymatic activity of Endothiapepsin in Complex with Compound TL00150 in 20% Dmso at 298 K:
3.4.23.22;

The structure of Endothiapepsin in Complex with Compound TL00150 in 20% Dmso at 298 K, PDB code: 7qm7 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)	37.37 / 1.79
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.003, 74.042, 53.55, 90, 109.79, 90
R / Rfree (%)	20.1 / 22.7

The binding sites of Fluorine atom in the Endothiapepsin in Complex with Compound TL00150 in 20% Dmso at 298 K (pdb code 7qm7). 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 20% Dmso at 298 K, PDB code: 7qm7:
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 20% 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 20% Dmso at 298 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F2805 b:52.7 occ:0.74 F08 A:U1H2805 0.0 52.7 0.7 C07 A:U1H2805 1.4 44.6 0.7 F10 A:U1H2805 2.2 46.6 0.7 F09 A:U1H2805 2.2 55.6 0.7 C06 A:U1H2805 2.4 36.3 0.7 C05 A:U1H2805 3.2 28.9 0.7 C11 A:U1H2805 3.2 37.4 0.7 C1 A:DMS2802 3.6 36.8 0.8 OD1 A:ASP119 3.7 55.7 1.0 C2 A:DMS2802 3.8 46.2 0.8 S A:DMS2802 4.2 40.2 0.8 C04 A:U1H2805 4.4 38.4 0.7 C12 A:U1H2805 4.4 36.9 0.7 CG A:ASP119 4.8 57.5 1.0 OD2 A:ASP81 4.9 56.8 1.0 C03 A:U1H2805 4.9 38.5 0.7

Fluorine binding site 2 out of 3 in the Endothiapepsin in Complex with Compound TL00150 in 20% 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 20% Dmso at 298 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F2805 b:55.6 occ:0.74 F09 A:U1H2805 0.0 55.6 0.7 C07 A:U1H2805 1.4 44.6 0.7 F08 A:U1H2805 2.2 52.7 0.7 F10 A:U1H2805 2.2 46.6 0.7 C06 A:U1H2805 2.4 36.3 0.7 C11 A:U1H2805 2.8 37.4 0.7 CE1 A:PHE116 3.5 34.0 1.0 C05 A:U1H2805 3.6 28.9 0.7 CD1 A:PHE116 3.7 32.9 1.0 OG A:SER115 3.8 54.6 1.0 OD1 A:ASP119 3.9 55.7 1.0 O A:SER115 3.9 41.6 1.0 CB A:SER115 4.0 55.1 1.0 C A:SER115 4.1 47.5 1.0 C12 A:U1H2805 4.1 36.9 0.7 OG A:SER83 4.2 63.0 1.0 CZ A:PHE116 4.3 35.1 1.0 CG A:PHE116 4.4 37.3 1.0 N A:PHE116 4.4 40.7 1.0 OD2 A:ASP81 4.5 56.8 1.0 CA A:PHE116 4.7 42.6 1.0 C04 A:U1H2805 4.7 38.4 0.7 CA A:SER115 4.7 48.3 1.0 CB A:SER83 4.8 44.5 1.0 CG A:ASP119 4.9 57.5 1.0 CE2 A:PHE116 4.9 43.7 1.0 C03 A:U1H2805 4.9 38.5 0.7 C2 A:DMS2802 5.0 46.2 0.8 CD2 A:PHE116 5.0 40.8 1.0

Fluorine binding site 3 out of 3 in the Endothiapepsin in Complex with Compound TL00150 in 20% 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 20% Dmso at 298 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F2805 b:46.6 occ:0.74 F10 A:U1H2805 0.0 46.6 0.7 C07 A:U1H2805 1.4 44.6 0.7 F08 A:U1H2805 2.2 52.7 0.7 F09 A:U1H2805 2.2 55.6 0.7 C06 A:U1H2805 2.4 36.3 0.7 C05 A:U1H2805 2.7 28.9 0.7 OD1 A:ASP119 3.6 55.7 1.0 C11 A:U1H2805 3.6 37.4 0.7 CD1 A:ILE122 3.6 33.6 1.0 CE1 A:PHE116 4.0 34.0 1.0 CD1 A:PHE116 4.0 32.9 1.0 C04 A:U1H2805 4.1 38.4 0.7 CG A:ASP119 4.3 57.5 1.0 CB A:ASP119 4.6 40.6 1.0 C12 A:U1H2805 4.7 36.9 0.7 OD2 A:ASP33 4.7 31.2 1.0 O A:SER115 4.9 41.6 1.0 C03 A:U1H2805 4.9 38.5 0.7 CG1 A:ILE122 4.9 28.6 1.0 C1 A:DMS2802 5.0 36.8 0.8 O A:HOH2963 5.0 37.4 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