Fluorine in PDB 1epr: Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040

All present enzymatic activity of Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040:
3.4.23.22;

The structure of Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040, PDB code: 1epr was solved by M.Badasso, M.Crawford, J.B.Cooper, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.090, 75.770, 43.010, 90.00, 97.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Fluorine atom in the Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040 (pdb code 1epr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040, PDB code: 1epr:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040 within 5.0Å range: probe atom residue distance (Å) B Occ E:F331 b:0.2 occ:1.00 F1 E:0QS331 0.0 0.2 1.0 CM1 E:0QS331 1.3 0.1 1.0 F2 E:0QS331 2.1 0.3 1.0 C6 E:0QS331 2.3 1.0 1.0 CH E:0QS331 2.3 -0.0 1.0 N1 E:0QS331 2.5 0.0 1.0 O2 E:0QS331 2.6 0.4 1.0 CA2 E:0QS331 2.8 0.4 1.0 C5 E:0QS331 2.9 0.4 1.0 OH1 E:0QS331 2.9 0.2 1.0 O1 E:0QS331 3.3 0.3 1.0 N2' E:0QS331 3.5 0.2 1.0 OG1 E:THR218 3.5 0.1 1.0 OH2 E:0QS331 3.5 0.6 1.0 OD2 E:ASP215 3.5 0.1 1.0 CA1 E:0QS331 3.7 -0.1 1.0 O E:HOH494 3.9 0.3 1.0 CD21 E:0QS331 4.0 0.5 1.0 CB2 E:0QS331 4.2 0.1 1.0 CB1 E:0QS331 4.3 0.6 1.0 CG1 E:0QS331 4.5 0.3 1.0 N E:GLY76 4.5 0.2 1.0 C2' E:0QS331 4.6 0.2 1.0 CG E:ASP215 4.7 -0.1 1.0 CD1 E:ILE301 4.9 0.2 1.0 CA E:GLY76 4.9 0.2 1.0 CB E:THR218 4.9 0.1 1.0 N E:0QS331 5.0 0.5 1.0

Fluorine binding site 2 out of 2 in the Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Endothia Aspartic Proteinase (Endothiapepsin) Complexed with Pd-135, 040 within 5.0Å range: probe atom residue distance (Å) B Occ E:F331 b:0.3 occ:1.00 F2 E:0QS331 0.0 0.3 1.0 CM1 E:0QS331 1.3 0.1 1.0 F1 E:0QS331 2.1 0.2 1.0 C6 E:0QS331 2.3 1.0 1.0 CH E:0QS331 2.3 -0.0 1.0 OH1 E:0QS331 2.6 0.2 1.0 N2' E:0QS331 2.6 0.2 1.0 OH2 E:0QS331 2.9 0.6 1.0 OD2 E:ASP215 3.1 0.1 1.0 O2 E:0QS331 3.4 0.4 1.0 O E:GLY34 3.4 0.2 1.0 CA2 E:0QS331 3.7 0.4 1.0 CA E:GLY34 3.8 -0.0 1.0 CG E:ASP215 3.9 -0.1 1.0 C E:GLY34 3.9 0.0 1.0 C2' E:0QS331 4.0 0.2 1.0 N1 E:0QS331 4.1 0.0 1.0 OD1 E:ASP215 4.2 0.0 1.0 O E:HOH494 4.2 0.3 1.0 CE1 E:PHE189 4.4 -0.1 1.0 OG1 E:THR218 4.5 0.1 1.0 CD1 E:ILE213 4.6 0.1 1.0 C1' E:0QS331 4.7 0.2 1.0 CB2 E:0QS331 4.8 0.1 1.0 C5 E:0QS331 4.8 0.4 1.0 OD1 E:ASP32 4.8 0.1 1.0 N E:GLY34 4.9 -0.0 1.0

D.Bailey, J.B.Cooper. A Structural Comparison of 21 Inhibitor Complexes of the Aspartic Proteinase From Endothia Parasitica. Protein Sci. V. 3 2129 1994.
ISSN: ISSN 0961-8368
PubMed: 7703859