Fluorine in PDB 1pfw: Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine

All present enzymatic activity of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine:
6.1.1.10;

The structure of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine, PDB code: 1pfw was solved by T.Crepin, E.Schmitt, Y.Mechulam, P.B.Sampson, M.D.Vaughan, J.F.Honek, S.Blanquet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 1.78
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.490, 45.288, 86.274, 90.00, 107.37, 90.00
R / Rfree (%)	18.4 / 20.9

The structure of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine (pdb code 1pfw). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine, PDB code: 1pfw:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:F553 b:20.0 occ:1.00 FZ1 A:MF3553 0.0 20.0 1.0 CE A:MF3553 1.4 20.9 1.0 FZ2 A:MF3553 2.2 19.1 1.0 FZ3 A:MF3553 2.4 20.2 1.0 SD A:MF3553 2.5 21.2 1.0 CG A:MF3553 2.8 23.5 1.0 CZ3 A:TRP253 3.3 31.8 1.0 CE2 A:PHE300 3.5 12.4 1.0 CE3 A:TRP253 3.7 30.6 1.0 CB A:ALA256 3.7 9.3 1.0 CD2 A:PHE300 3.9 12.7 1.0 N A:PRO257 4.0 10.1 1.0 CD A:PRO257 4.0 9.7 1.0 CB A:MF3553 4.1 23.7 1.0 CE1 A:HIS301 4.1 9.3 1.0 CH2 A:TRP253 4.2 31.1 1.0 CZ A:PHE300 4.3 15.6 1.0 C A:ALA256 4.3 9.3 1.0 CB A:PRO257 4.4 10.1 1.0 CA A:PRO257 4.4 9.4 1.0 NE2 A:HIS301 4.5 8.9 1.0 CA A:ALA256 4.7 9.5 1.0 CG A:PRO257 4.7 11.1 1.0 CD2 A:TRP253 4.8 30.2 1.0 O A:HOH1173 4.9 20.4 1.0 OD2 A:ASP52 4.9 13.8 1.0 O A:ALA256 4.9 8.7 1.0 OH A:TYR260 5.0 5.5 1.0 CA A:MF3553 5.0 24.2 1.0

Fluorine binding site 2 out of 3 in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:F553 b:19.1 occ:1.00 FZ2 A:MF3553 0.0 19.1 1.0 CE A:MF3553 1.4 20.9 1.0 FZ3 A:MF3553 2.2 20.2 1.0 FZ1 A:MF3553 2.2 20.0 1.0 SD A:MF3553 2.5 21.2 1.0 OH A:TYR260 3.1 5.5 1.0 CE1 A:TYR260 3.2 6.8 1.0 CZ A:TYR260 3.2 5.9 1.0 NE2 A:HIS301 3.3 8.9 1.0 CA A:PRO257 3.3 9.4 1.0 CB A:PRO257 3.4 10.1 1.0 CE1 A:HIS301 3.6 9.3 1.0 N A:PRO257 3.7 10.1 1.0 CG A:MF3553 3.9 23.5 1.0 CD1 A:TYR260 4.0 6.6 1.0 CE2 A:TYR260 4.1 6.6 1.0 C A:ALA256 4.2 9.3 1.0 CD A:PRO257 4.2 9.7 1.0 CE2 A:PHE300 4.3 12.4 1.0 O A:ALA256 4.3 8.7 1.0 CD2 A:HIS301 4.4 9.4 1.0 CG A:PRO257 4.5 11.1 1.0 C A:PRO257 4.7 9.7 1.0 CG A:LEU13 4.7 8.8 1.0 CD2 A:PHE300 4.8 12.7 1.0 ND1 A:HIS301 4.8 8.2 1.0 CG A:TYR260 4.8 6.5 1.0 CB A:ALA256 4.8 9.3 1.0 CD2 A:TYR260 4.8 6.1 1.0

Fluorine binding site 3 out of 3 in the Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Methionyl-Trna Synthetase From Escherichia Coli Complexed with Trifluoromethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:F553 b:20.2 occ:1.00 FZ3 A:MF3553 0.0 20.2 1.0 CE A:MF3553 1.4 20.9 1.0 FZ2 A:MF3553 2.2 19.1 1.0 FZ1 A:MF3553 2.4 20.0 1.0 SD A:MF3553 2.5 21.2 1.0 CG A:MF3553 3.0 23.5 1.0 O A:ALA256 3.1 8.7 1.0 C A:ALA256 3.2 9.3 1.0 N A:PRO257 3.4 10.1 1.0 CB A:ALA256 3.4 9.3 1.0 CG A:LEU13 3.4 8.8 1.0 CD1 A:LEU13 3.5 10.7 1.0 CA A:PRO257 3.7 9.4 1.0 CA A:ALA256 3.8 9.5 1.0 CB A:LEU13 3.8 8.8 1.0 CD A:PRO257 4.3 9.7 1.0 N A:LEU13 4.4 7.9 1.0 CZ A:TYR260 4.4 5.9 1.0 CB A:PRO257 4.5 10.1 1.0 CB A:MF3553 4.5 23.7 1.0 OH A:TYR260 4.5 5.5 1.0 OD2 A:ASP52 4.5 13.8 1.0 CE1 A:TYR260 4.7 6.8 1.0 CA A:LEU13 4.7 9.1 1.0 CE2 A:TYR260 4.7 6.6 1.0 CD2 A:LEU13 4.8 8.1 1.0 C A:PRO257 4.9 9.7 1.0

T.Crepin, E.Schmitt, Y.Mechulam, P.B.Sampson, M.D.Vaughan, J.F.Honek, S.Blanquet. Use of Analogues of Methionine and Methionyl Adenylate to Sample Conformational Changes During Catalysis in Escherichia Coli Methionyl-Trna Synthetase. J.Mol.Biol. V. 332 59 2003.
ISSN: ISSN 0022-2836
PubMed: 12946347
DOI: 10.1016/S0022-2836(03)00917-3