Fluorine in PDB 7h5r: Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K

All present enzymatic activity of Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K:
3.4.23.22;

The structure of Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K, PDB code: 7h5r was solved by C.-Y.Huang, S.Aumonier, V.Olieric, M.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.46, 74, 53.36, 90, 110.12, 90
R / Rfree (%)	20.1 / 23.3

The binding sites of Fluorine atom in the Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K (pdb code 7h5r). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K, PDB code: 7h5r:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K


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 Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F903 b:44.4 occ:0.84 F08 A:U1H903 0.0 44.4 0.8 C07 A:U1H903 1.4 44.1 0.8 F10 A:U1H903 2.2 44.3 0.8 F09 A:U1H903 2.3 44.2 0.8 C06 A:U1H903 2.4 43.5 0.8 C05 A:U1H903 2.8 43.4 0.8 OD2 A:ASP119 3.4 44.5 1.0 CE1 A:PHE116 3.5 30.0 1.0 CD1 A:PHE116 3.6 29.8 1.0 C11 A:U1H903 3.6 43.1 0.8 CD1 A:ILE122 3.9 25.2 1.0 C04 A:U1H903 4.1 43.1 0.8 CG A:ASP119 4.2 43.0 1.0 CB A:ASP119 4.4 35.9 1.0 O A:SER115 4.4 32.0 1.0 CZ A:PHE116 4.5 29.6 1.0 CG A:PHE116 4.6 29.3 1.0 O A:HOH1059 4.6 23.4 1.0 O A:HOH1111 4.7 40.9 1.0 C12 A:U1H903 4.7 42.9 0.8 CA A:PHE116 4.7 29.9 1.0 C A:SER115 4.8 32.0 1.0 CG2 A:ILE122 4.9 25.3 1.0 C03 A:U1H903 4.9 42.6 0.8 N A:PHE116 4.9 30.7 1.0 CB A:ILE122 5.0 25.2 1.0 CG1 A:ILE122 5.0 25.1 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K


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 Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F903 b:44.2 occ:0.84 F09 A:U1H903 0.0 44.2 0.8 C07 A:U1H903 1.4 44.1 0.8 F10 A:U1H903 2.2 44.3 0.8 F08 A:U1H903 2.3 44.4 0.8 C06 A:U1H903 2.4 43.5 0.8 C05 A:U1H903 3.2 43.4 0.8 O A:HOH1331 3.3 35.1 1.0 C11 A:U1H903 3.3 43.1 0.8 OD2 A:ASP119 3.6 44.5 1.0 C1 A:DMS905 3.8 26.9 0.7 O A:HOH1111 3.9 40.9 1.0 C2 A:DMS905 4.0 26.8 0.7 C04 A:U1H903 4.4 43.1 0.8 C12 A:U1H903 4.5 42.9 0.8 O A:HOH1185 4.5 57.2 1.0 CG A:ASP119 4.5 43.0 1.0 S A:DMS905 4.6 27.0 0.7 OD2 A:ASP81 4.6 40.1 1.0 OG A:SER115 4.7 38.1 1.0 CB A:SER115 4.8 34.2 1.0 O A:SER115 4.8 32.0 1.0 C03 A:U1H903 5.0 42.6 0.8

Fluorine binding site 3 out of 3 in the Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Endothiapepsin IS_CRYO3 in Complex with TL00150 at 100 K within 5.0Å range: probe atom residue distance (Å) B Occ A:F903 b:44.3 occ:0.84 F10 A:U1H903 0.0 44.3 0.8 C07 A:U1H903 1.4 44.1 0.8 F09 A:U1H903 2.2 44.2 0.8 F08 A:U1H903 2.2 44.4 0.8 C06 A:U1H903 2.4 43.5 0.8 C11 A:U1H903 2.7 43.1 0.8 OG A:SER115 3.0 38.1 1.0 CE1 A:PHE116 3.6 30.0 1.0 CB A:SER115 3.6 34.2 1.0 C05 A:U1H903 3.6 43.4 0.8 CD1 A:PHE116 3.7 29.8 1.0 C A:SER115 3.8 32.0 1.0 O A:SER115 4.0 32.0 1.0 CZ A:PHE116 4.0 29.6 1.0 N A:PHE116 4.0 30.7 1.0 C12 A:U1H903 4.1 42.9 0.8 CG A:PHE116 4.2 29.3 1.0 OD2 A:ASP81 4.2 40.1 1.0 O A:HOH1111 4.2 40.9 1.0 CB A:SER83 4.2 32.2 1.0 OG A:SER83 4.3 34.4 1.0 CA A:SER115 4.3 32.4 1.0 CE2 A:PHE116 4.4 29.6 1.0 CA A:PHE116 4.4 29.9 1.0 CD2 A:PHE116 4.5 28.9 1.0 O A:HOH1185 4.5 57.2 1.0 OD2 A:ASP119 4.7 44.5 1.0 C04 A:U1H903 4.7 43.1 0.8 C03 A:U1H903 4.9 42.6 0.8 CB A:PHE116 4.9 29.2 1.0

C.Y.Huang, S.Aumonier, V.Olieric, M.Wang. CRYO2RT: A High-Throughput Method For Room-Temperature Macromolecular Crystallography From Cryocooled Crystals. Acta Crystallogr D Struct 2024BIOL.
ISSN: ISSN 2059-7983
PubMed: 39052318
DOI: 10.1107/S2059798324006697