Fluorine in PDB 4y4e: Endothiapepsin in Complex with Fragment 131

All present enzymatic activity of Endothiapepsin in Complex with Fragment 131:
3.4.23.22;

The structure of Endothiapepsin in Complex with Fragment 131, PDB code: 4y4e was solved by S.G.Krimmer, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.61 / 1.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.273, 73.192, 52.781, 90.00, 109.43, 90.00
R / Rfree (%)	11.4 / 13.6

The binding sites of Fluorine atom in the Endothiapepsin in Complex with Fragment 131 (pdb code 4y4e). 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 Fragment 131, PDB code: 4y4e:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Endothiapepsin in Complex with Fragment 131


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 Fragment 131 within 5.0Å range: probe atom residue distance (Å) B Occ A:F403 b:43.2 occ:1.00 F2 A:46R403 0.0 43.2 1.0 C6 A:46R403 1.3 42.5 1.0 F1 A:46R403 2.1 41.4 1.0 F A:46R403 2.1 42.6 1.0 C5 A:46R403 2.4 42.2 1.0 N A:46R403 2.9 41.6 1.0 HD11 A:ILE217 2.9 10.9 1.0 HD13 A:ILE217 3.2 10.9 1.0 HZ A:PHE194 3.3 15.2 1.0 HE2 A:PHE194 3.3 13.9 1.0 CD1 A:ILE217 3.4 9.1 1.0 CZ A:PHE194 3.4 12.7 1.0 CE2 A:PHE194 3.4 11.6 1.0 HD12 A:ILE217 3.6 10.9 1.0 C4 A:46R403 3.8 41.6 1.0 O A:GLY37 4.2 9.3 1.0 O A:46R403 4.2 41.7 1.0 HG21 A:ILE302 4.2 22.3 1.0 OD1 A:ASP219 4.3 12.8 1.0 CE1 A:PHE194 4.3 13.1 1.0 CD2 A:PHE194 4.3 10.0 1.0 HA3 A:GLY37 4.4 8.8 1.0 HD11 A:ILE304 4.5 11.6 1.0 HD13 A:ILE304 4.5 11.6 1.0 HE1 A:PHE194 4.7 15.8 1.0 HD2 A:PHE194 4.7 12.1 1.0 HG12 A:ILE304 4.7 9.6 1.0 C3 A:46R403 4.8 41.2 1.0 N1 A:46R403 4.8 40.7 1.0 CG1 A:ILE217 4.8 8.5 1.0 CD1 A:ILE304 4.9 9.7 1.0 HA2 A:GLY37 5.0 8.8 1.0 O A:HOH501 5.0 13.6 1.0 CD1 A:PHE194 5.0 11.6 1.0 HG12 A:ILE217 5.0 10.2 1.0

Fluorine binding site 2 out of 3 in the Endothiapepsin in Complex with Fragment 131


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 Fragment 131 within 5.0Å range: probe atom residue distance (Å) B Occ A:F403 b:42.6 occ:1.00 F A:46R403 0.0 42.6 1.0 C6 A:46R403 1.3 42.5 1.0 F1 A:46R403 2.1 41.4 1.0 F2 A:46R403 2.1 43.2 1.0 C5 A:46R403 2.4 42.2 1.0 O A:46R403 2.8 41.7 1.0 N A:46R403 2.9 41.6 1.0 C4 A:46R403 3.0 41.6 1.0 HA3 A:GLY80 3.2 29.4 1.0 H A:GLY80 3.4 27.1 1.0 CA A:GLY80 3.9 24.5 1.0 N A:GLY80 4.0 22.6 1.0 HA2 A:GLY80 4.1 29.4 1.0 C3 A:46R403 4.2 41.2 1.0 HZ A:PHE194 4.2 15.2 1.0 HD11 A:ILE304 4.6 11.6 1.0 HE2 A:PHE194 4.7 13.9 1.0 HD11 A:ILE217 4.8 10.9 1.0 CZ A:PHE194 4.8 12.7 1.0 N1 A:46R403 4.8 40.7 1.0 HD13 A:ILE304 4.8 11.6 1.0 HA A:TYR79 5.0 21.9 1.0

Fluorine binding site 3 out of 3 in the Endothiapepsin in Complex with Fragment 131


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 Fragment 131 within 5.0Å range: probe atom residue distance (Å) B Occ A:F403 b:41.4 occ:1.00 F1 A:46R403 0.0 41.4 1.0 C6 A:46R403 1.3 42.5 1.0 F A:46R403 2.1 42.6 1.0 F2 A:46R403 2.1 43.2 1.0 C5 A:46R403 2.4 42.2 1.0 HD13 A:ILE304 2.9 11.6 1.0 HD11 A:ILE304 3.1 11.6 1.0 HD11 A:ILE217 3.4 10.9 1.0 CD1 A:ILE304 3.5 9.7 1.0 OD1 A:ASP219 3.5 12.8 1.0 N A:46R403 3.7 41.6 1.0 HA3 A:GLY80 4.0 29.4 1.0 HG1 A:THR222 4.0 11.8 1.0 OG1 A:THR222 4.1 9.8 1.0 HG12 A:ILE304 4.1 9.6 1.0 HD12 A:ILE304 4.2 11.6 1.0 CD1 A:ILE217 4.2 9.1 1.0 O A:46R403 4.3 41.7 1.0 C4 A:46R403 4.4 41.6 1.0 HG21 A:ILE304 4.4 8.4 1.0 HD13 A:ILE217 4.4 10.9 1.0 CG1 A:ILE304 4.4 8.0 1.0 O A:HOH501 4.4 13.6 1.0 H A:GLY80 4.5 27.1 1.0 HD12 A:ILE217 4.5 10.9 1.0 CG A:ASP219 4.7 9.4 1.0 HG23 A:ILE304 4.8 8.4 1.0 HG21 A:ILE302 4.8 22.3 1.0 CA A:GLY80 4.9 24.5 1.0 CG2 A:ILE304 5.0 7.0 1.0

S.G.Krimmer, A.Heine, G.Klebe. Crystallographic Fragment Screening of An Entire Library To Be Published.