Fluorine in PDB 7uz2: Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide.

The structure of Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide., PDB code: 7uz2 was solved by P.M.Danby, A.Jeong, L.Sim, R.P.Sweeney, J.F.Wardman, A.Geissner, L.J.Worrall, N.C.J.Strynadka, S.G.Withers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.42 / 1.83
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	168.265, 168.265, 95.504, 90, 90, 120
R / Rfree (%)	20.7 / 24.2

The binding sites of Fluorine atom in the Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide. (pdb code 7uz2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide., PDB code: 7uz2:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide. within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:42.6 occ:1.00 F5A A:OML501 0.0 42.6 1.0 C5A A:OML501 1.4 35.7 1.0 H2 A:OML501 2.3 35.0 1.0 C5 A:OML501 2.3 35.1 1.0 C1 A:OML501 2.4 34.8 1.0 H4 A:OML501 2.5 34.6 1.0 C6 A:OML501 2.7 34.8 1.0 HD2 A:TYR322 3.1 49.7 1.0 OE2 A:GLU387 3.1 34.8 1.0 OE1 A:GLU387 3.3 39.1 1.0 HH2 A:TRP361 3.3 32.6 1.0 O6 A:OML501 3.4 35.2 1.0 CD A:GLU387 3.5 41.0 1.0 HZ3 A:TRP361 3.5 33.6 1.0 HE2 A:TYR322 3.5 48.6 1.0 H3 A:OML501 3.5 35.0 1.0 CD2 A:TYR322 3.5 52.5 1.0 C2 A:OML501 3.7 32.7 1.0 O A:HOH607 3.7 39.8 1.0 C4 A:OML501 3.7 30.9 1.0 CE2 A:TYR322 3.7 45.6 1.0 H6 A:OML501 3.9 33.3 1.0 H1 A:OML501 3.9 35.3 0.0 CH2 A:TRP361 4.0 31.5 1.0 CZ3 A:TRP361 4.1 35.8 1.0 H10 A:OML501 4.1 31.8 1.0 C3 A:OML501 4.2 32.8 1.0 H8 A:OML501 4.3 32.1 1.0 HB3 A:TYR322 4.4 39.6 1.0 CG A:TYR322 4.5 47.9 1.0 HG2 A:GLU387 4.6 40.5 1.0 CG A:GLU387 4.7 41.3 1.0 O4 A:OML501 4.8 29.8 1.0 O2 A:OML501 4.8 33.6 1.0 HE2 A:PHE441 4.8 29.4 1.0 CZ A:TYR322 4.8 51.3 1.0 OE2 A:GLU206 4.8 45.0 1.0 HZ A:PHE441 4.8 29.5 1.0 H11 A:OML501 4.8 29.9 0.0

Fluorine binding site 2 out of 2 in the Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Beta-Glycosidase From Sulfolobus Solfataricus in Complex with C5A-Fluoro-Valienide. within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:49.2 occ:1.00 F5A B:OML501 0.0 49.2 1.0 C5A B:OML501 1.3 42.6 1.0 C5 B:OML501 2.3 38.7 1.0 C1 B:OML501 2.4 41.1 1.0 H2 B:OML501 2.5 36.6 1.0 H4 B:OML501 2.5 40.9 1.0 C6 B:OML501 2.8 36.5 1.0 OE1 B:GLU387 3.0 48.5 1.0 OE2 B:GLU387 3.0 39.8 1.0 HD2 B:TYR322 3.0 56.1 1.0 CD B:GLU387 3.3 47.5 1.0 O6 B:OML501 3.5 34.8 1.0 HE2 B:TYR322 3.5 55.8 1.0 HH2 B:TRP361 3.6 37.6 1.0 CD2 B:TYR322 3.6 57.9 1.0 H3 B:OML501 3.7 36.6 1.0 C2 B:OML501 3.7 39.5 1.0 C4 B:OML501 3.7 35.5 1.0 HZ3 B:TRP361 3.7 39.3 1.0 CE2 B:TYR322 3.8 54.8 1.0 H6 B:OML501 3.9 39.6 1.0 H1 B:OML501 4.1 34.8 0.0 C3 B:OML501 4.1 38.0 1.0 H10 B:OML501 4.2 36.2 1.0 CH2 B:TRP361 4.2 35.1 1.0 H8 B:OML501 4.2 37.2 1.0 CZ3 B:TRP361 4.3 42.6 1.0 HB3 B:TYR322 4.5 47.2 1.0 HG2 B:GLU387 4.5 44.0 1.0 CG B:GLU387 4.5 45.0 1.0 CG B:TYR322 4.6 53.8 1.0 OE2 B:GLU206 4.6 56.2 1.0 O4 B:OML501 4.7 33.5 1.0 O2 B:OML501 4.8 40.3 1.0 H11 B:OML501 4.8 33.5 0.0 HE2 B:PHE441 4.9 31.8 1.0 CZ B:TYR322 5.0 56.5 1.0 HG3 B:GLU387 5.0 44.0 1.0

P.M.Danby, A.Jeong, L.Sim, R.P.Sweeney, J.F.Wardman, R.Karimi, A.Geissner, L.J.Worrall, J.P.Reid, N.C.J.Strynadka, S.Withers. Vinyl Halide-Modified Unsaturated Cyclitols Are Mechanism-Based Glycosidase Inhibitors. Angew.Chem.Int.Ed.Engl. 01258 2023.
ISSN: ESSN 1521-3773
PubMed: 36940280
DOI: 10.1002/ANIE.202301258