Fluorine in PDB 3hzh: Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi

The structure of Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi, PDB code: 3hzh was solved by Y.Pazy, R.E.Silversmith, M.Guarinari, R.Zhao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.64 / 1.96
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	63.705, 63.705, 175.685, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 25.9

The structure of Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi (pdb code 3hzh). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi, PDB code: 3hzh:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi


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 Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ A:F79 b:26.2 occ:1.00 F1 A:BFD79 0.0 26.2 1.0 BE A:BFD79 1.5 28.8 1.0 MG A:MG202 2.1 30.2 1.0 F2 A:BFD79 2.4 26.0 1.0 F3 A:BFD79 2.4 25.4 1.0 OD1 A:BFD79 2.5 25.5 1.0 OD2 A:BFD79 2.7 27.9 1.0 CG A:BFD79 2.9 28.6 1.0 O A:HOH157 3.0 41.9 1.0 OD1 B:ASN99 3.0 22.1 1.0 O A:THR81 3.1 20.6 1.0 O B:HOH162 3.2 34.6 1.0 CB A:THR81 3.3 23.2 1.0 N A:THR81 3.4 22.9 1.0 O A:HOH158 3.5 41.9 1.0 CA A:THR81 3.6 21.7 1.0 CG B:ASN99 3.7 24.4 1.0 ND2 B:ASN99 3.7 24.0 1.0 C A:THR81 3.8 24.2 1.0 OG1 A:THR81 3.9 18.9 1.0 OD1 A:ASP33 4.1 17.6 1.0 N A:ILE80 4.3 23.0 1.0 NZ A:LYS129 4.3 21.4 1.0 CG2 A:THR81 4.4 19.8 1.0 C A:ILE80 4.4 23.6 1.0 CB A:BFD79 4.4 25.2 1.0 O B:HOH192 4.7 41.7 1.0 OG A:SER107 4.8 25.5 1.0 CA A:ILE80 4.9 24.5 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi


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 Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ A:F79 b:26.0 occ:1.00 F2 A:BFD79 0.0 26.0 1.0 BE A:BFD79 1.5 28.8 1.0 F1 A:BFD79 2.4 26.2 1.0 OD1 A:BFD79 2.4 25.5 1.0 F3 A:BFD79 2.5 25.4 1.0 OG A:SER107 2.6 25.5 1.0 O B:HOH162 2.9 34.6 1.0 N A:THR81 2.9 22.9 1.0 N A:ILE80 3.1 23.0 1.0 CB A:SER107 3.2 22.5 1.0 CG A:BFD79 3.4 28.6 1.0 CB A:ILE80 3.4 23.3 1.0 CA A:ILE80 3.5 24.5 1.0 OG1 A:THR81 3.7 18.9 1.0 C A:ILE80 3.7 23.6 1.0 N A:ALA108 3.7 21.9 1.0 CA A:SER107 3.8 24.0 1.0 CB A:THR81 3.8 23.2 1.0 OD2 A:BFD79 3.9 27.9 1.0 CA A:THR81 3.9 21.7 1.0 C A:BFD79 4.3 25.1 1.0 C A:SER107 4.3 23.1 1.0 MG A:MG202 4.3 30.2 1.0 CG1 A:ILE80 4.4 24.5 1.0 CG2 A:ILE80 4.4 24.7 1.0 OD1 B:ASN99 4.6 22.1 1.0 O A:THR81 4.6 20.6 1.0 CB A:BFD79 4.6 25.2 1.0 CA A:BFD79 4.6 25.4 1.0 N A:LEU109 4.6 22.4 1.0 CD1 A:LEU109 4.6 28.0 1.0 C A:THR81 4.7 24.2 1.0 O A:HOH150 4.7 47.0 1.0 CG A:LEU109 4.8 23.8 1.0 CB A:ALA108 4.8 21.0 1.0 CA A:ALA108 4.8 21.8 1.0 O A:ILE106 4.8 26.9 1.0 O A:ILE80 4.9 22.2 1.0 ND2 B:ASN99 4.9 24.0 1.0 O A:HOH157 5.0 41.9 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi within 5.0Å range: probe atom residue distance (Å) B Occ A:F79 b:25.4 occ:1.00 F3 A:BFD79 0.0 25.4 1.0 BE A:BFD79 1.5 28.8 1.0 F1 A:BFD79 2.4 26.2 1.0 F2 A:BFD79 2.5 26.0 1.0 OD1 A:BFD79 2.5 25.5 1.0 N A:ALA108 2.9 21.9 1.0 NZ A:LYS129 2.9 21.4 1.0 OD1 B:ASN99 3.0 22.1 1.0 CE A:LYS129 3.4 21.6 1.0 O B:HOH162 3.4 34.6 1.0 CA A:SER107 3.5 24.0 1.0 CD A:LYS129 3.6 22.4 1.0 CB A:ALA108 3.6 21.0 1.0 CG A:BFD79 3.6 28.6 1.0 O A:HOH157 3.6 41.9 1.0 C A:SER107 3.6 23.1 1.0 OG A:SER107 3.7 25.5 1.0 CA A:ALA108 3.8 21.8 1.0 CB A:SER107 3.9 22.5 1.0 CG B:ASN99 4.1 24.4 1.0 OD2 A:BFD79 4.1 27.9 1.0 MG A:MG202 4.2 30.2 1.0 ND2 B:ASN99 4.4 24.0 1.0 O A:ILE106 4.4 26.9 1.0 CG A:LYS129 4.7 23.6 1.0 N A:SER107 4.7 24.8 1.0 OD2 A:ASP32 4.8 19.0 1.0 O A:SER107 4.8 24.0 1.0 CB A:BFD79 4.8 25.2 1.0 OE1 B:GLU96 4.8 27.3 1.0 OE2 B:GLU96 4.8 25.5 1.0 N A:ILE80 4.8 23.0 1.0 C A:ALA108 4.9 23.9 1.0 N A:LEU109 4.9 22.4 1.0

Y.Pazy, M.A.Motaleb, M.T.Guarnieri, N.W.Charon, R.Zhao, R.E.Silversmith. Identical Phosphatase Mechanisms Achieved Through Distinct Modes of Binding Phosphoprotein Substrate. Proc.Natl.Acad.Sci.Usa V. 107 1924 2010.
ISSN: ISSN 0027-8424
PubMed: 20080618
DOI: 10.1073/PNAS.0911185107