Fluorine in PDB 2pu1: Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah)

All present enzymatic activity of Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah):
4.2.1.11;

The structure of Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah), PDB code: 2pu1 was solved by M.V.A.S.Navarro, D.J.Rigden, R.C.Garratt, S.M.G.Dias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.04 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	74.809, 110.644, 109.006, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 20.6

The structure of Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah) also contains other interesting chemical elements:

Zinc

(Zn)

3 atoms

The binding sites of Fluorine atom in the Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah) (pdb code 2pu1). 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 T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah), PDB code: 2pu1:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah)


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 T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah) within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:20.7 occ:0.50 F A:FSG600 0.0 20.7 0.5 C1 A:FSG600 1.2 15.6 0.5 C1 A:FSG600 1.4 17.9 0.5 F A:FSG600 1.9 15.3 0.5 C2 A:FSG600 2.2 16.6 0.5 C2 A:FSG600 2.3 17.5 0.5 P A:FSG600 2.5 16.1 0.5 P A:FSG600 2.6 17.9 0.5 O2 A:FSG600 2.6 17.7 0.5 O3P A:FSG600 2.7 18.5 0.5 OG A:SER40 2.7 17.5 1.0 OE1 A:GLN164 2.7 23.9 1.0 O2 A:FSG600 2.7 15.6 0.5 O3P A:FSG600 2.8 19.1 0.5 CD A:GLN164 3.0 24.8 1.0 NE2 A:GLN164 3.0 21.0 1.0 O A:HOH760 3.2 19.6 1.0 O2P A:FSG600 3.2 18.2 0.5 N3 A:FSG600 3.3 16.6 0.5 O2P A:FSG600 3.3 18.3 0.5 N3 A:FSG600 3.4 16.2 0.5 ZN A:ZN501 3.5 21.9 1.0 O1P A:FSG600 3.6 15.4 0.5 O1P A:FSG600 3.8 19.1 0.5 OE2 A:GLU165 4.0 21.3 1.0 CB A:SER40 4.0 20.6 1.0 CG A:GLN164 4.1 22.5 1.0 CB A:SER373 4.2 14.3 1.0 OG A:SER373 4.3 17.3 1.0 O A:HOH722 4.4 16.3 1.0 N A:SER40 4.4 20.1 1.0 O3 A:FSG600 4.5 19.3 0.5 O3 A:FSG600 4.5 16.1 0.5 OE2 A:GLU208 4.6 20.7 1.0 O A:HOH727 4.6 18.8 1.0 CA A:SER40 4.7 20.4 1.0 O A:HOH851 4.8 32.3 1.0 ZN A:ZN500 4.9 21.2 1.0 OD2 A:ASP243 4.9 16.5 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah)


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 T. Brucei Enolase Complexed with Fluoro-Phosphonoacetohydroxamate (Fpah) within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:15.3 occ:0.50 F A:FSG600 0.0 15.3 0.5 C1 A:FSG600 1.1 17.9 0.5 C1 A:FSG600 1.3 15.6 0.5 F A:FSG600 1.9 20.7 0.5 C2 A:FSG600 2.2 17.5 0.5 C2 A:FSG600 2.3 16.6 0.5 N3 A:FSG600 2.5 16.2 0.5 N3 A:FSG600 2.5 16.6 0.5 P A:FSG600 2.6 17.9 0.5 P A:FSG600 2.6 16.1 0.5 O A:HOH722 2.7 16.3 1.0 O1P A:FSG600 2.8 15.4 0.5 O1P A:FSG600 2.9 19.1 0.5 O A:HOH760 2.9 19.6 1.0 OE2 A:GLU208 3.0 20.7 1.0 O3P A:FSG600 3.1 19.1 0.5 O3P A:FSG600 3.2 18.5 0.5 O2 A:FSG600 3.2 17.7 0.5 O2 A:FSG600 3.4 15.6 0.5 CB A:SER373 3.4 14.3 1.0 OE2 A:GLU165 3.5 21.3 1.0 O2P A:FSG600 3.6 18.2 0.5 N A:SER373 3.7 14.8 1.0 O2P A:FSG600 3.7 18.3 0.5 OE1 A:GLN164 3.8 23.9 1.0 O3 A:FSG600 3.9 16.1 0.5 O3 A:FSG600 3.9 19.3 0.5 CA A:SER373 3.9 15.7 1.0 OG A:SER373 4.0 17.3 1.0 CD A:GLU208 4.2 18.8 1.0 CD A:GLN164 4.4 24.8 1.0 OG A:SER40 4.5 17.5 1.0 C A:ARG372 4.5 14.9 1.0 ZN A:ZN501 4.6 21.9 1.0 CD A:GLU165 4.7 19.6 1.0 OE1 A:GLU208 4.8 17.7 1.0 NE2 A:GLN164 4.8 21.0 1.0 NZ A:LYS343 4.8 15.4 1.0 CA A:ARG372 4.9 14.2 1.0

M.V.Navarro, S.M.Gomes Dias, L.V.Mello, M.T.Da Silva Giotto, S.Gavalda, C.Blonski, R.C.Garratt, D.J.Rigden. Structural Flexibility in Trypanosoma Brucei Enolase Revealed By X-Ray Crystallography and Molecular Dynamics. Febs J. V. 274 5077 2007.
ISSN: ISSN 1742-464X
PubMed: 17822439
DOI: 10.1111/J.1742-4658.2007.06027.X