Fluorine in PDB 2vs2: Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor.

All present enzymatic activity of Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor.:
3.4.23.22;

The binding sites of Fluorine atom in the Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor. (pdb code 2vs2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor., PDB code: 2vs2:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:15.7 occ:1.00 F1 A:0QS400 0.0 15.7 1.0 CM1 A:0QS400 1.3 15.0 1.0 F2 A:0QS400 2.1 14.6 1.0 HD21 A:0QS400 2.3 35.7 1.0 C6 A:0QS400 2.3 18.3 1.0 CH A:0QS400 2.3 13.6 1.0 N1 A:0QS400 2.7 15.3 1.0 O2 A:0QS400 2.8 17.9 1.0 CA2 A:0QS400 2.8 13.3 1.0 OH1 A:0QS400 2.9 10.7 1.0 C5 A:0QS400 2.9 24.5 1.0 CD21 A:0QS400 3.0 34.8 1.0 HA2 A:0QS400 3.0 14.4 1.0 HD2 A:ASP219 3.1 9.0 0.3 DD2 A:ASP219 3.1 9.0 0.7 O1 A:0QS400 3.2 23.2 1.0 N2' A:0QS400 3.5 26.0 1.0 HG1 A:THR222 3.5 9.8 0.3 DG1 A:THR222 3.5 9.8 0.7 OH2 A:0QS400 3.5 12.2 1.0 OD2 A:ASP219 3.5 10.5 1.0 NE2 A:0QS400 3.6 37.3 1.0 HE21 A:0QS400 3.6 36.8 1.0 D A:GLY80 3.7 15.3 0.6 H A:GLY80 3.7 15.3 0.5 OG1 A:THR222 3.7 10.6 1.0 DH1 A:0QS400 3.9 11.7 1.0 CG1 A:0QS400 3.9 33.5 1.0 HA3 A:GLY80 4.0 16.5 1.0 HA1 A:0QS400 4.0 26.0 1.0 CA1 A:0QS400 4.0 26.2 1.0 HD12 A:ILE304 4.3 10.1 1.0 CB2 A:0QS400 4.3 14.6 1.0 HH2 A:0QS400 4.4 12.7 0.8 DH2 A:0QS400 4.4 12.7 0.2 HB22 A:0QS400 4.5 13.4 1.0 N A:GLY80 4.5 15.1 1.0 CB1 A:0QS400 4.5 29.3 1.0 HA3 A:GLY37 4.5 6.1 1.0 HD1 A:TYR79 4.6 11.3 1.0 HB3 A:TYR79 4.6 10.3 1.0 CE11 A:0QS400 4.7 37.5 1.0 CG A:ASP219 4.7 6.7 1.0 HB31 A:0QS400 4.8 14.3 1.0 CA A:GLY80 4.8 16.4 1.0 C2' A:0QS400 4.8 31.2 1.0 ND1 A:0QS400 4.9 36.6 1.0 H2'2 A:0QS400 4.9 30.9 1.0 HD11 A:ILE304 4.9 10.0 1.0 HB3 A:0QS400 4.9 29.7 1.0 HD13 A:ILE217 4.9 11.3 1.0

Fluorine binding site 2 out of 2 in the Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Neutron Diffraction Structure of Endothiapepsin in Complex with A Gem- Diol Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:F400 b:14.6 occ:1.00 F2 A:0QS400 0.0 14.6 1.0 CM1 A:0QS400 1.3 15.0 1.0 F1 A:0QS400 2.1 15.7 1.0 CH A:0QS400 2.3 13.6 1.0 C6 A:0QS400 2.3 18.3 1.0 OH1 A:0QS400 2.5 10.7 1.0 N2' A:0QS400 2.7 26.0 1.0 HA3 A:GLY37 2.7 6.1 1.0 OH2 A:0QS400 2.9 12.2 1.0 OD2 A:ASP219 3.0 10.5 1.0 HD2 A:ASP219 3.1 9.0 0.3 DD2 A:ASP219 3.1 9.0 0.7 DH1 A:0QS400 3.2 11.7 1.0 O A:GLY37 3.3 7.8 1.0 O2 A:0QS400 3.4 17.9 1.0 CA A:GLY37 3.6 7.1 1.0 HH2 A:0QS400 3.6 12.7 0.8 DH2 A:0QS400 3.6 12.7 0.2 CA2 A:0QS400 3.7 13.3 1.0 C A:GLY37 3.7 5.7 1.0 HE1 A:PHE194 3.8 11.7 1.0 HD13 A:ILE217 3.9 11.3 1.0 CG A:ASP219 3.9 6.7 1.0 HA2 A:GLY37 4.0 6.2 1.0 HA2 A:0QS400 4.0 14.4 1.0 HD21 A:0QS400 4.1 35.7 1.0 N1 A:0QS400 4.1 15.3 1.0 C2' A:0QS400 4.1 31.2 1.0 OD1 A:ASP219 4.3 8.1 1.0 H2'2 A:0QS400 4.6 30.9 1.0 HD11 A:ILE217 4.6 12.2 1.0 CE1 A:PHE194 4.6 12.1 1.0 H2'1 A:0QS400 4.6 30.7 1.0 HB3 A:SER38 4.6 9.6 1.0 OG1 A:THR222 4.6 10.6 1.0 CD1 A:ILE217 4.6 12.1 1.0 H1'2 A:0QS400 4.7 33.4 1.0 OD1 A:ASP35 4.7 5.8 1.0 H1'1 A:0QS400 4.7 33.1 1.0 N A:GLY37 4.7 5.8 1.0 C1' A:0QS400 4.8 33.6 1.0 HD1 A:TYR79 4.8 11.3 1.0 HG1 A:THR222 4.8 9.8 0.3 DG1 A:THR222 4.8 9.8 0.7 HD12 A:ILE217 4.8 11.5 1.0 C5 A:0QS400 4.8 24.5 1.0 CD21 A:0QS400 4.8 34.8 1.0 CB2 A:0QS400 4.8 14.6 1.0 HB22 A:0QS400 4.8 13.4 1.0 N A:SER38 4.8 6.7 1.0 HB2 A:ASP219 4.9 6.8 1.0 D A:GLY37 4.9 6.5 0.3 H A:GLY37 4.9 6.5 0.7 HD12 A:ILE304 4.9 10.1 1.0 HE21 A:0QS400 4.9 36.8 1.0 HB31 A:0QS400 5.0 14.3 1.0 D A:GLY80 5.0 15.3 0.6 H A:GLY80 5.0 15.3 0.5 OD2 A:ASP35 5.0 8.5 1.0

L.Coates, H.-F.Tuan, S.Tomanicek, A.Kovalevsky, M.Mustyakimov, P.Erskine, J.Cooper. The Catalytic Mechanism of An Aspartic Proteinase Explored with Neutron and X-Ray Diffraction J.Am.Chem.Soc. V. 130 7235 2008.
ISSN: ISSN 0002-7863
PubMed: 18479128
DOI: 10.1021/JA801269X