Fluorine in PDB 6n5g: Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2

The structure of Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2, PDB code: 6n5g was solved by G.S.Oliveira, P.P.Adriani, J.A.Ribeiro, C.Morisseau, B.D.Hammock, M.V.Dias, F.S.Chambergo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.81 / 2.60
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.420, 77.323, 86.703, 90.00, 90.00, 90.00
R / Rfree (%)	27 / 34

The binding sites of Fluorine atom in the Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2 (pdb code 6n5g). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2, PDB code: 6n5g:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:26.9 occ:1.00 F10 A:KDS401 0.0 26.9 1.0 C09 A:KDS401 1.4 26.8 1.0 F12 A:KDS401 2.2 26.6 1.0 F11 A:KDS401 2.2 28.3 1.0 O08 A:KDS401 2.3 28.0 1.0 C07 A:KDS401 2.4 26.2 1.0 C13 A:KDS401 3.0 25.4 1.0 C06 A:KDS401 3.0 30.4 1.0 ND1 A:HIS313 3.7 30.2 1.0 C14 A:KDS401 3.9 28.7 1.0 C05 A:KDS401 3.9 33.5 1.0 CB A:ALA288 4.0 35.3 1.0 CG A:HIS313 4.0 26.7 1.0 CB A:HIS313 4.0 30.6 1.0 C04 A:KDS401 4.3 36.7 1.0 OD1 A:ASN287 4.4 38.2 1.0 CE2 A:PHE205 4.4 23.5 1.0 CE1 A:HIS313 4.4 32.4 1.0 CD2 A:PHE205 4.7 20.0 1.0 CD2 A:HIS313 4.8 34.4 1.0 NE1 A:TRP314 5.0 23.4 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:28.3 occ:1.00 F11 A:KDS401 0.0 28.3 1.0 C09 A:KDS401 1.4 26.8 1.0 F12 A:KDS401 2.2 26.6 1.0 F10 A:KDS401 2.2 26.9 1.0 O08 A:KDS401 2.3 28.0 1.0 C07 A:KDS401 3.1 26.2 1.0 O A:MET193 3.2 19.5 1.0 NE1 A:TRP314 3.3 23.4 1.0 C13 A:KDS401 3.3 25.4 1.0 CZ2 A:TRP314 3.6 20.5 1.0 CE2 A:TRP314 3.7 20.4 1.0 CE A:MET193 3.7 18.9 1.0 ND1 A:HIS313 4.2 30.2 1.0 C A:MET193 4.2 21.4 1.0 C06 A:KDS401 4.3 30.4 1.0 CD1 A:TRP314 4.3 25.3 1.0 CA A:MET193 4.6 25.3 1.0 C14 A:KDS401 4.6 28.7 1.0 CH2 A:TRP314 4.7 27.4 1.0 CD2 A:TRP314 4.8 24.6 1.0 CD2 A:PHE205 4.9 20.0 1.0 CB A:MET193 4.9 23.9 1.0 CE1 A:HIS313 4.9 32.4 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:26.6 occ:1.00 F12 A:KDS401 0.0 26.6 1.0 C09 A:KDS401 1.4 26.8 1.0 F10 A:KDS401 2.2 26.9 1.0 F11 A:KDS401 2.2 28.3 1.0 O08 A:KDS401 2.3 28.0 1.0 CD2 A:PHE205 3.0 20.0 1.0 CE2 A:PHE205 3.3 23.5 1.0 C07 A:KDS401 3.4 26.2 1.0 CG A:PHE205 3.9 20.9 1.0 C06 A:KDS401 4.0 30.4 1.0 CE A:MET193 4.1 18.9 1.0 C13 A:KDS401 4.3 25.4 1.0 CB A:PHE205 4.3 16.5 1.0 O A:MET193 4.4 19.5 1.0 CZ A:PHE205 4.4 23.3 1.0 OD1 A:ASN287 4.7 38.2 1.0 CD1 A:PHE205 4.8 16.5 1.0 ND2 A:ASN287 5.0 24.3 1.0

G.S.De Oliveira, P.P.Adriani, J.A.Ribeiro, C.Morisseau, B.D.Hammock, M.V.B.Dias, F.S.Chambergo. The Molecular Structure of An Epoxide Hydrolase From Trichoderma Reesei in Complex with Urea or Amide-Based Inhibitors. Int. J. Biol. Macromol. V. 129 653 2019.
ISSN: ISSN 1879-0003
PubMed: 30771398
DOI: 10.1016/J.IJBIOMAC.2019.02.070