Fluorine in PDB 5rc7: Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A

All present enzymatic activity of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A:
3.4.23.22;

The structure of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A, PDB code: 5rc7 was solved by M.S.Weiss, J.Wollenhaupt, A.Metz, T.Barthel, G.M.A.Lima, A.Heine, U.Mueller, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.58 / 0.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.186, 73.094, 52.386, 90.00, 109.02, 90.00
R / Rfree (%)	15.6 / 15.7

The binding sites of Fluorine atom in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A (pdb code 5rc7). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A, PDB code: 5rc7:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:16.4 occ:0.18 F A:AES401 0.0 16.4 0.2 F A:AES401 0.0 16.4 0.2 S A:AES401 1.5 15.9 0.2 S A:AES401 1.5 15.9 0.2 O1S A:AES401 2.4 16.7 0.2 O1S A:AES401 2.4 16.7 0.2 O2S A:AES401 2.4 17.1 0.2 O2S A:AES401 2.4 17.1 0.2 C1 A:AES401 2.5 14.3 0.2 C1 A:AES401 2.5 14.3 0.2 C2 A:AES401 3.2 14.5 0.2 C2 A:AES401 3.2 14.5 0.2 OD2 A:ASP81 3.2 28.0 0.3 OD2 A:ASP81 3.2 28.0 0.3 C6 A:AES401 3.4 13.0 0.2 C6 A:AES401 3.4 13.0 0.2 C1 A:DMS403 3.5 24.8 0.9 C2 A:DMS403 3.6 17.1 0.9 S A:DMS403 4.0 18.3 0.9 OD2 A:ASP81 4.1 17.9 0.2 OD2 A:ASP81 4.1 17.9 0.2 CB A:SER115 4.3 17.1 0.2 CB A:SER115 4.3 17.1 0.2 OD1 A:ASP119 4.3 23.3 0.2 OD1 A:ASP119 4.3 23.5 0.2 CG A:ASP81 4.4 26.2 0.3 CG A:ASP81 4.4 26.2 0.3 C3 A:AES401 4.5 14.0 0.2 C3 A:AES401 4.5 14.0 0.2 OG A:SER115 4.5 19.6 0.2 OG A:SER115 4.5 19.6 0.2 C5 A:AES401 4.6 12.1 0.2 C5 A:AES401 4.6 12.1 0.2 CB A:SER115 4.9 18.8 0.3 CB A:SER115 4.9 18.8 0.3 O A:HOH505 5.0 33.5 1.0 CG A:ASP81 5.0 17.7 0.2 CG A:ASP81 5.0 17.7 0.2

Fluorine binding site 2 out of 2 in the Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Pandda Analysis Group Deposition -- Endothiapepsin Changed State Model For Fragment F2X-Entry Library F11A within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:16.4 occ:0.18 F A:AES401 0.0 16.4 0.2 F A:AES401 0.0 16.4 0.2 S A:AES401 1.5 15.9 0.2 S A:AES401 1.5 15.9 0.2 O1S A:AES401 2.4 16.7 0.2 O1S A:AES401 2.4 16.7 0.2 O2S A:AES401 2.4 17.1 0.2 O2S A:AES401 2.4 17.1 0.2 C1 A:AES401 2.5 14.3 0.2 C1 A:AES401 2.5 14.3 0.2 C2 A:AES401 3.2 14.5 0.2 C2 A:AES401 3.2 14.5 0.2 OD2 A:ASP81 3.2 28.0 0.3 OD2 A:ASP81 3.2 28.0 0.3 C6 A:AES401 3.4 13.0 0.2 C6 A:AES401 3.4 13.0 0.2 C1 A:DMS403 3.5 24.8 0.9 C2 A:DMS403 3.6 17.1 0.9 S A:DMS403 4.0 18.3 0.9 OD2 A:ASP81 4.1 17.9 0.2 OD2 A:ASP81 4.1 17.9 0.2 CB A:SER115 4.3 17.1 0.2 CB A:SER115 4.3 17.1 0.2 OD1 A:ASP119 4.3 23.3 0.2 OD1 A:ASP119 4.3 23.5 0.2 CG A:ASP81 4.4 26.2 0.3 CG A:ASP81 4.4 26.2 0.3 C3 A:AES401 4.5 14.0 0.2 C3 A:AES401 4.5 14.0 0.2 OG A:SER115 4.5 19.6 0.2 OG A:SER115 4.5 19.6 0.2 C5 A:AES401 4.6 12.1 0.2 C5 A:AES401 4.6 12.1 0.2 CB A:SER115 4.9 18.8 0.3 CB A:SER115 4.9 18.8 0.3 O A:HOH505 5.0 33.5 1.0 CG A:ASP81 5.0 17.7 0.2 CG A:ASP81 5.0 17.7 0.2

J.Wollenhaupt, A.Metz, T.Barthel, G.M.A.Lima, A.Heine, U.Mueller, G.Klebe, M.S.Weiss. F2X-Universal and F2X-Entry: Structurally Diverse Compound Libraries For Crystallographic Fragment Screening. Structure 2020.
ISSN: ISSN 0969-2126
PubMed: 32413289
DOI: 10.1016/J.STR.2020.04.019