Fluorine in PDB 3ssv: Engineered Low-Affinity Halide-Binding Protein Derived From Yfp: Fluoride Complex

The structure of Engineered Low-Affinity Halide-Binding Protein Derived From Yfp: Fluoride Complex, PDB code: 3ssv was solved by W.Wang, J.S.Grimley, L.S.Beese, H.W.Hellinga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.80 / 1.86
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.444, 62.865, 70.086, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 21.3

The binding sites of Fluorine atom in the Engineered Low-Affinity Halide-Binding Protein Derived From Yfp: Fluoride Complex (pdb code 3ssv). 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 Engineered Low-Affinity Halide-Binding Protein Derived From Yfp: Fluoride Complex, PDB code: 3ssv:

Fluorine binding site 1 out of 1 in the Engineered Low-Affinity Halide-Binding Protein Derived From Yfp: Fluoride Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Engineered Low-Affinity Halide-Binding Protein Derived From Yfp: Fluoride Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F260 b:23.7 occ:1.00 HD21 A:ASN185 1.9 25.6 1.0 HE22 A:GLN69 1.9 21.6 1.0 HE22 A:GLN94 2.1 24.4 1.0 O A:HOH263 2.5 20.2 1.0 NE2 A:GLN69 2.7 18.0 1.0 ND2 A:ASN185 2.7 21.4 1.0 HE21 A:GLN183 2.9 25.8 1.0 HE2 A:PHE84 2.9 24.4 1.0 NE2 A:GLN94 2.9 20.3 1.0 HG3 A:GLN94 2.9 26.0 1.0 HE22 A:GLN183 3.1 25.8 1.0 HE21 A:GLN69 3.1 21.6 1.0 HD22 A:ASN185 3.1 25.6 1.0 HG3 A:GLN69 3.2 25.4 1.0 HE1 A:TYR92 3.2 23.6 1.0 NE2 A:GLN183 3.2 21.5 1.0 HB2 A:GLN69 3.2 23.7 1.0 HB2 A:GLN94 3.3 24.6 1.0 HH A:TYR92 3.4 22.9 1.0 HE21 A:GLN94 3.4 24.4 1.0 CD A:GLN69 3.6 22.8 1.0 CG A:GLN94 3.6 21.7 1.0 CE2 A:PHE84 3.6 20.3 1.0 CG A:GLN69 3.7 21.1 1.0 CD A:GLN94 3.7 22.4 1.0 CG A:ASN185 3.7 24.1 1.0 H A:GLN69 3.8 22.0 1.0 CE1 A:TYR92 3.8 19.7 1.0 OD1 A:ASN185 3.9 24.8 1.0 HD2 A:PHE84 3.9 23.1 1.0 CB A:GLN69 3.9 19.8 1.0 CB A:GLN94 4.0 20.6 1.0 OH A:TYR92 4.1 19.1 1.0 CD2 A:PHE84 4.1 19.3 1.0 CZ A:TYR92 4.3 20.4 1.0 CD A:GLN183 4.3 22.6 1.0 O A:HOH297 4.3 22.1 1.0 HG2 A:GLN94 4.5 26.0 1.0 HB3 A:GLN94 4.5 24.6 1.0 HB3 A:GLN69 4.5 23.7 1.0 CZ A:PHE84 4.6 19.6 1.0 N A:GLN69 4.6 18.4 1.0 HG2 A:GLN69 4.6 25.4 1.0 HZ A:PHE84 4.7 23.5 1.0 OE1 A:GLN69 4.7 25.0 1.0 CD1 A:TYR92 4.8 20.9 1.0 HD1 A:TYR92 4.9 25.1 1.0 OE1 A:GLN94 4.9 23.0 1.0 CA A:GLN69 4.9 19.2 1.0 O2 A:CR266 4.9 18.1 1.0 OE1 A:GLN183 4.9 21.6 1.0 HH21 A:ARG96 5.0 23.5 1.0 HD11 A:ILE161 5.0 34.1 1.0 HA A:GLN94 5.0 25.9 1.0

W.Wang, J.S.Grimley, G.J.Augustine, L.S.Beese, H.W.Hellinga. Determination of Engineered Chloride-Binding Site Structures in Fluorescent Proteins Reveals Principles of Halide Recognition To Be Published.