Fluorine in PDB 1od1: Endothiapepsin PD135,040 Complex

All present enzymatic activity of Endothiapepsin PD135,040 Complex:
3.4.23.22;

The structure of Endothiapepsin PD135,040 Complex, PDB code: 1od1 was solved by L.Coates, P.T.Erskine, S.Mall, R.S.Gill, S.P.Wood, J.B.Cooper, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.37
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.201, 73.249, 45.993, 90.00, 110.10, 90.00
R / Rfree (%)	12.5 / 15.9

The binding sites of Fluorine atom in the Endothiapepsin PD135,040 Complex (pdb code 1od1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Endothiapepsin PD135,040 Complex, PDB code: 1od1:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Endothiapepsin PD135,040 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Endothiapepsin PD135,040 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:29.2 occ:1.00 F1 A:0QS400 0.0 29.2 1.0 CM1 A:0QS400 1.3 20.0 1.0 F2 A:0QS400 2.1 27.0 1.0 C6 A:0QS400 2.3 19.5 1.0 CH A:0QS400 2.4 17.3 1.0 O2 A:0QS400 2.7 22.2 1.0 OH1 A:0QS400 3.0 16.4 1.0 CA2 A:0QS400 3.0 15.2 1.0 N1 A:0QS400 3.0 14.8 1.0 CD21 A:0QS400 3.3 34.6 1.0 N2' A:0QS400 3.3 18.1 1.0 C5 A:0QS400 3.3 14.1 1.0 OH2 A:0QS400 3.5 15.7 1.0 NE2 A:0QS400 3.5 41.8 1.0 O1 A:0QS400 3.5 16.6 1.0 OD2 A:ASP219 3.7 18.4 1.0 OG1 A:THR222 3.9 15.8 1.0 CG1 A:0QS400 4.0 29.1 1.0 CA1 A:0QS400 4.3 13.3 1.0 N A:GLY80 4.3 17.0 1.0 CE11 A:0QS400 4.4 42.0 1.0 CB2 A:0QS400 4.5 14.3 1.0 CA A:GLY80 4.5 18.1 1.0 C2' A:0QS400 4.6 20.6 1.0 ND1 A:0QS400 4.7 36.5 1.0 CB1 A:0QS400 4.8 19.5 1.0 CG A:ASP219 4.8 12.3 1.0

Fluorine binding site 2 out of 2 in the Endothiapepsin PD135,040 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Endothiapepsin PD135,040 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:27.0 occ:1.00 F2 A:0QS400 0.0 27.0 1.0 CM1 A:0QS400 1.3 20.0 1.0 F1 A:0QS400 2.1 29.2 1.0 CH A:0QS400 2.3 17.3 1.0 C6 A:0QS400 2.4 19.5 1.0 OH1 A:0QS400 2.5 16.4 1.0 N2' A:0QS400 2.5 18.1 1.0 OH2 A:0QS400 2.8 15.7 1.0 OD2 A:ASP219 3.0 18.4 1.0 O A:GLY37 3.2 13.4 1.0 O2 A:0QS400 3.4 22.2 1.0 CA A:GLY37 3.5 11.0 1.0 C A:GLY37 3.6 10.2 1.0 CA2 A:0QS400 3.7 15.2 1.0 CG A:ASP219 3.9 12.3 1.0 C2' A:0QS400 4.0 20.6 1.0 OD1 A:ASP219 4.2 14.7 1.0 N1 A:0QS400 4.3 14.8 1.0 OD1 A:ASP35 4.6 11.5 1.0 CD1 A:ILE217 4.6 18.0 1.0 CE1 A:PHE194 4.7 16.4 1.0 N A:GLY37 4.7 9.8 1.0 OG1 A:THR222 4.7 15.8 1.0 C1' A:0QS400 4.7 21.6 1.0 N A:SER38 4.7 10.3 1.0 CB2 A:0QS400 4.8 14.3 1.0 OD2 A:ASP35 4.9 13.3 1.0

L.Coates, P.T.Erskine, S.Mall, P.A.Williams, R.S.Gill, S.P.Wood, J.B.Cooper. The Structure of Endothiapepsin Complexed with the Gem-Diol Inhibitor Pd-135,040 at 1.37 A Acta Crystallogr.,Sect.D V. 59 978 2003.
ISSN: ISSN 0907-4449
PubMed: 12777758
DOI: 10.1107/S0907444903006267