Fluorine in PDB 3eon: 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule

All present enzymatic activity of 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule:
1.3.99.7;

The structure of 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule, PDB code: 3eon was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.63 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	97.409, 106.169, 144.185, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 26.6

The binding sites of Fluorine atom in the 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule (pdb code 3eon). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule, PDB code: 3eon:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule within 5.0Å range: probe atom residue distance (Å) B Occ C:F501 b:74.3 occ:1.00 F8 C:341501 0.0 74.3 1.0 C1 C:341501 1.3 74.7 1.0 C6 C:341501 2.4 74.8 1.0 C2 C:341501 2.4 74.3 1.0 NZ C:LYS331 2.9 37.9 1.0 CE C:LYS331 3.1 36.8 1.0 O C:VAL370 3.3 33.5 1.0 C5 C:341501 3.6 74.9 1.0 C3 C:341501 3.6 74.5 1.0 OE2 C:GLU374 3.9 41.1 1.0 CB C:TYR373 4.0 40.0 1.0 CG C:GLU374 4.0 40.6 1.0 CD1 C:ILE257 4.1 34.3 1.0 C4 C:341501 4.1 74.5 1.0 CD C:GLU374 4.1 41.5 1.0 CD2 C:TYR373 4.2 43.7 1.0 C C:VAL370 4.4 33.7 1.0 CG1 C:VAL370 4.4 30.6 1.0 CG C:TYR373 4.5 42.8 1.0 CD C:LYS331 4.6 34.8 1.0 CG2 C:ILE257 4.7 31.0 1.0 F7 C:341501 4.7 74.8 1.0 CA C:VAL370 4.8 32.4 1.0 N C:GLU374 4.8 40.1 1.0 C9 C:341501 4.9 73.9 1.0 CB C:GLU374 4.9 40.7 1.0 CA C:TYR373 5.0 39.8 1.0 OE1 C:GLU374 5.0 41.0 1.0

Fluorine binding site 2 out of 2 in the 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of 2.55A Crystal Structure of Native Glutaryl-Coa Dehydrogenase From Burkholderia Pseudomallei in Complex with A Small Molecule within 5.0Å range: probe atom residue distance (Å) B Occ C:F501 b:74.8 occ:1.00 F7 C:341501 0.0 74.8 1.0 C3 C:341501 1.3 74.5 1.0 C2 C:341501 2.4 74.3 1.0 C4 C:341501 2.4 74.5 1.0 C1 C:341501 3.6 74.7 1.0 C5 C:341501 3.7 74.9 1.0 CD2 C:LEU250 3.9 33.8 1.0 CE2 C:TYR373 3.9 42.8 1.0 C6 C:341501 4.1 74.8 1.0 CD2 C:TYR373 4.2 43.7 1.0 CD1 C:ILE257 4.5 34.3 1.0 CB C:ALA253 4.5 30.2 1.0 F8 C:341501 4.7 74.3 1.0 CD1 C:LEU106 4.8 27.6 1.0 CZ C:TYR373 4.9 43.5 1.0 C9 C:341501 4.9 73.9 1.0

D.W.Begley, D.R.Davies, R.C.Hartley, S.N.Hewitt, A.L.Rychel, P.J.Myler, W.C.Van Voorhis, B.L.Staker, L.J.Stewart. Probing Conformational States of Glutaryl-Coa Dehydrogenase By Fragment Screening. Acta Crystallogr.,Sect.F V. 67 1060 2011.
ISSN: ESSN 1744-3091
PubMed: 21904051
DOI: 10.1107/S1744309111014436