Fluorine in PDB 2rhw: Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda

The structure of Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda, PDB code: 2rhw was solved by S.Bhowmik, J.T.Bolin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.80 / 1.57
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	117.956, 117.956, 87.193, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 20

The structure of Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda (pdb code 2rhw). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda, PDB code: 2rhw:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda


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 the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda within 5.0Å range: probe atom residue distance (Å) B Occ A:F288 b:27.4 occ:0.60 FA3 A:C0E288 0.0 27.4 0.6 CA3 A:C0E288 1.3 59.5 0.6 C1 A:MLI2 1.6 25.4 0.4 CA2 A:C0E288 2.3 59.0 0.6 CA4 A:C0E288 2.4 38.0 0.6 C3 A:MLI2 2.5 12.8 0.4 OA3 A:C0E288 2.7 72.2 0.6 CA5 A:C0E288 2.8 16.3 0.6 C2 A:MLI2 2.9 51.6 0.4 O8 A:MLI2 2.9 27.9 0.4 CD1 A:LEU156 3.0 20.1 0.5 CD2 A:LEU156 3.2 38.5 0.5 O6 A:MLI2 3.3 32.8 0.4 O9 A:MLI2 3.5 34.6 0.4 CG A:LEU156 3.6 21.6 0.5 CD1 A:LEU156 3.6 22.6 0.5 CE1 A:PHE239 3.6 17.4 1.0 CD1 A:PHE239 3.6 15.9 1.0 CA1 A:C0E288 3.6 69.7 0.6 CD2 A:HIS265 3.7 10.4 0.5 CE1 A:PHE175 3.9 31.6 1.0 O7 A:MLI2 3.9 43.4 0.4 OA2 A:C0E288 4.1 77.5 0.6 NE2 A:HIS265 4.1 11.2 0.5 CA A:GLY43 4.1 18.6 1.0 N A:GLY43 4.2 17.3 1.0 CA6 A:C0E288 4.2 22.4 0.6 CD1 A:PHE175 4.2 24.6 1.0 ND1 A:HIS265 4.4 56.7 0.5 CZ A:PHE239 4.6 18.0 1.0 OA1 A:C0E288 4.6 39.5 0.6 CG A:PHE239 4.6 14.9 1.0 CZ A:PHE175 4.8 27.8 1.0 CG A:LEU156 4.8 16.4 0.5 OA4 A:C0E288 4.8 11.9 0.6 CE1 A:HIS265 4.9 61.7 0.5 CB A:LEU156 5.0 22.6 0.5 CB A:LEU156 5.0 11.9 0.5

Fluorine binding site 2 out of 2 in the Crystal Structure of the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda


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 the S112A Mutant of A C-C Hydrolase, Bphd From Burkholderia Xenovorans LB400, in Complex with 3,10-Di-Fluoro Hopda within 5.0Å range: probe atom residue distance (Å) B Occ A:F288 b:44.2 occ:0.60 FB4 A:C0E288 0.0 44.2 0.6 CB4 A:C0E288 1.3 22.1 0.6 CB3 A:C0E288 2.4 22.0 0.6 CB5 A:C0E288 2.4 22.2 0.6 O A:HOH414 2.9 17.5 1.0 N A:GLY139 3.0 18.8 1.0 CD2 A:LEU213 3.0 37.3 1.0 CD1 A:LEU213 3.2 36.4 1.0 CG A:LEU213 3.5 38.2 1.0 CA A:GLY138 3.5 16.0 1.0 CB6 A:C0E288 3.6 19.2 0.6 CB2 A:C0E288 3.6 20.7 0.6 C A:GLY138 3.7 22.1 1.0 O A:HOH417 3.7 20.9 1.0 CA A:GLY139 3.8 20.1 1.0 CB1 A:C0E288 4.1 19.4 0.6 O A:HOH416 4.5 23.3 1.0 CG1 A:VAL240 4.5 8.5 0.5 O A:GLY138 4.8 19.6 1.0 CD1 A:ILE153 4.8 24.0 1.0 O A:HOH412 4.9 17.3 1.0 N A:GLY138 4.9 15.1 1.0 CB A:LEU213 5.0 32.4 1.0

S.Bhowmik, G.P.Horsman, J.T.Bolin, L.D.Eltis. The Molecular Basis For Inhibition of Bphd, A C-C Bond Hydrolase Involved in Polychlorinated Biphenyls Degradation: Large 3-Substituents Prevent Tautomerization. J.Biol.Chem. V. 282 36377 2007.
ISSN: ISSN 0021-9258
PubMed: 17932031
DOI: 10.1074/JBC.M707035200