Fluorine in PDB 1bjg: D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring

All present enzymatic activity of D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring:
2.1.1.45;

The structure of D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring, PDB code: 1bjg was solved by C.R.Sage, M.D.Michelitsch, J.Finer-Moore, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.30
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	133.000, 133.000, 133.000, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.4

The binding sites of Fluorine atom in the D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring (pdb code 1bjg). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring, PDB code: 1bjg:

Fluorine binding site 1 out of 1 in the D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of D221(169)N Mutant Does Not Promote Opening of the Cofactor Imidazolidine Ring within 5.0Å range: probe atom residue distance (Å) B Occ A:F266 b:62.3 occ:0.58 F5 A:UFP266 0.0 62.3 0.6 C2 A:TMF267 1.4 50.4 0.4 C5 A:UFP266 1.4 57.9 0.6 N3 A:TMF267 1.8 47.5 0.4 NA2 A:TMF267 1.9 53.1 0.4 N1 A:TMF267 2.2 50.5 0.4 C4 A:UFP266 2.5 57.9 0.6 C6 A:UFP266 2.5 53.6 0.6 C4 A:TMF267 2.7 47.2 0.4 O4 A:UFP266 2.8 58.8 0.6 C8A A:TMF267 2.9 49.4 0.4 SG A:CYS146 3.0 47.1 1.0 C4A A:TMF267 3.2 49.4 0.4 OH A:TYR94 3.3 14.3 1.0 CB A:CYS146 3.3 24.8 1.0 N3 A:UFP266 3.7 57.3 0.6 N1 A:UFP266 3.7 55.4 0.6 O4 A:TMF267 3.8 41.1 0.4 N8 A:TMF267 4.0 49.0 0.4 N A:CYS146 4.0 16.4 1.0 C2 A:UFP266 4.2 57.0 0.6 CA A:CYS146 4.3 17.3 1.0 CD2 A:HIS147 4.4 16.9 1.0 CZ A:TYR94 4.4 14.4 1.0 NE2 A:HIS147 4.5 13.7 1.0 N5 A:TMF267 4.6 50.4 0.4 CD1 A:LEU143 4.6 34.6 1.0 CE2 A:TYR94 4.7 12.0 1.0 C1' A:UFP266 4.9 56.1 0.6

C.R.Sage, M.D.Michelitsch, T.J.Stout, D.Biermann, R.Nissen, J.Finer-Moore, R.M.Stroud. D221 in Thymidylate Synthase Controls Conformation Change, and Thereby Opening of the Imidazolidine. Biochemistry V. 37 13893 1998.
ISSN: ISSN 0006-2960
PubMed: 9753479
DOI: 10.1021/BI9810510