Fluorine in PDB 5bp0: X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)

The structure of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650), PDB code: 5bp0 was solved by J.Bobango, B.Sankaran, J.F.Park, J.Wu, T.T.Talley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.16 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	82.470, 129.040, 122.430, 90.00, 106.28, 90.00
R / Rfree (%)	19.8 / 24.8

The binding sites of Fluorine atom in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) (pdb code 5bp0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 8 binding sites of Fluorine where determined in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650), PDB code: 5bp0:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Fluorine binding site 1 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:45.4 occ:1.00 F13 A:FN1302 0.0 45.4 1.0 C4 A:FN1302 1.3 55.4 1.0 C3 A:FN1302 2.3 53.1 1.0 HD23 B:LEU112 2.4 52.9 1.0 HG3 B:ARG104 2.4 48.8 1.0 H3 A:FN1302 2.5 63.7 1.0 C5 A:FN1302 2.5 40.8 1.0 H5 A:FN1302 2.7 49.0 1.0 HG2 B:ARG104 2.7 48.8 1.0 CG B:ARG104 3.0 40.6 1.0 HG A:CYS188 3.2 72.1 1.0 HD21 B:LEU112 3.2 52.9 1.0 CD2 B:LEU112 3.2 44.1 1.0 HB2 B:ARG104 3.4 50.2 1.0 HG B:LEU112 3.6 53.0 1.0 C2 A:FN1302 3.6 41.4 1.0 N1 A:FN1302 3.7 37.3 1.0 HH A:TYR192 3.7 69.2 1.0 CB B:ARG104 3.8 41.8 1.0 HA A:THR144 3.9 45.1 1.0 HD22 B:LEU112 4.0 52.9 1.0 CG B:LEU112 4.0 44.2 1.0 HB A:THR144 4.0 50.4 1.0 OH A:TYR192 4.1 57.7 1.0 HB3 B:LEU112 4.1 42.9 1.0 C1 A:FN1302 4.1 48.9 1.0 SG A:CYS188 4.1 60.1 1.0 HG22 A:THR144 4.2 46.0 1.0 CD B:ARG104 4.2 47.5 1.0 HB3 B:ARG104 4.3 50.2 1.0 HD3 B:ARG104 4.3 57.0 1.0 H6 A:FN1302 4.5 71.4 1.0 CB B:LEU112 4.6 35.7 1.0 CA A:THR144 4.7 37.6 1.0 O A:THR144 4.7 43.8 1.0 CB A:THR144 4.7 42.0 1.0 H B:ARG104 4.7 45.1 1.0 HE B:ARG104 4.7 57.6 1.0 C6 A:FN1302 4.8 59.5 1.0 NE B:ARG104 4.8 48.0 1.0 CG2 A:THR144 4.9 38.3 1.0 O B:LEU112 4.9 37.3 1.0 CA B:ARG104 5.0 35.5 1.0 HD2 B:ARG104 5.0 57.0 1.0 N B:ARG104 5.0 37.6 1.0

Fluorine binding site 2 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ B:F303 b:56.4 occ:1.00 F13 B:FN1303 0.0 56.4 1.0 C4 B:FN1303 1.3 52.8 1.0 C3 B:FN1303 2.3 56.7 1.0 H3 B:FN1303 2.5 68.1 1.0 C5 B:FN1303 2.5 46.6 1.0 H5 B:FN1303 2.7 55.9 1.0 HG3 C:ARG104 2.9 34.1 1.0 HG2 C:ARG104 3.0 34.1 1.0 CG C:ARG104 3.4 28.4 1.0 C2 B:FN1303 3.7 54.3 1.0 N1 B:FN1303 3.7 52.2 1.0 HA B:THR144 3.8 38.0 1.0 HB B:THR144 4.1 36.5 1.0 HB2 C:ARG104 4.1 38.8 1.0 C1 B:FN1303 4.2 56.2 1.0 HG22 B:THR144 4.2 36.9 1.0 HD3 C:ARG104 4.2 44.9 1.0 OH B:TYR192 4.2 48.7 1.0 CD C:ARG104 4.4 37.4 1.0 CB C:ARG104 4.4 32.4 1.0 HH B:TYR192 4.5 58.4 1.0 HB2 C:LEU112 4.6 39.3 1.0 HB3 C:LEU112 4.6 39.3 1.0 H6 B:FN1303 4.6 71.5 1.0 CA B:THR144 4.6 31.7 1.0 HB3 C:MET114 4.7 43.0 1.0 CB B:THR144 4.7 30.4 1.0 O C:LEU112 4.7 33.9 1.0 O C:HOH430 4.8 35.2 1.0 O B:TRP143 4.8 34.4 1.0 C6 B:FN1303 4.8 59.6 1.0 O B:THR144 4.8 35.0 1.0 H72 B:FN1303 4.9 63.6 1.0 CG2 B:THR144 4.9 30.7 1.0 HE C:ARG104 4.9 42.1 1.0 H C:ARG104 4.9 34.7 1.0 HD13 C:LEU112 4.9 78.0 1.0 HE2 C:MET114 5.0 53.8 1.0 HD12 C:LEU112 5.0 78.0 1.0

Fluorine binding site 3 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ C:F302 b:52.3 occ:1.00 F13 C:FN1302 0.0 52.3 1.0 C4 C:FN1302 1.3 49.9 1.0 C3 C:FN1302 2.3 49.6 1.0 HG3 D:ARG104 2.5 48.7 1.0 C5 C:FN1302 2.5 40.9 1.0 H3 C:FN1302 2.5 59.5 1.0 H5 C:FN1302 2.7 49.0 1.0 HD23 D:LEU112 2.8 60.5 1.0 HG2 D:ARG104 3.0 48.7 1.0 CG D:ARG104 3.1 40.6 1.0 HH C:TYR192 3.3 75.2 1.0 HD21 D:LEU112 3.3 60.5 1.0 HB2 D:ARG104 3.4 45.5 1.0 CD2 D:LEU112 3.5 50.4 1.0 OH C:TYR192 3.7 62.7 1.0 N1 C:FN1302 3.7 47.0 1.0 C2 C:FN1302 3.7 50.0 1.0 HG D:LEU112 3.7 59.4 1.0 HA C:THR144 3.8 40.8 1.0 CB D:ARG104 3.8 37.9 1.0 HB C:THR144 4.1 42.3 1.0 CG D:LEU112 4.1 49.5 1.0 C1 C:FN1302 4.2 48.2 1.0 HG22 C:THR144 4.3 47.7 1.0 HD22 D:LEU112 4.3 60.5 1.0 HB3 D:ARG104 4.3 45.5 1.0 SG C:CYS188 4.3 63.6 1.0 CD D:ARG104 4.3 44.7 1.0 HD3 D:ARG104 4.4 53.6 1.0 HB3 D:LEU112 4.5 43.8 1.0 O C:THR144 4.5 48.2 1.0 CA C:THR144 4.6 34.0 1.0 H6 C:FN1302 4.6 57.7 1.0 H D:ARG104 4.6 40.9 1.0 HE D:ARG104 4.6 53.3 1.0 H103 C:FN1302 4.7 53.5 1.0 CB C:THR144 4.7 35.3 1.0 CZ C:TYR192 4.8 58.7 1.0 C6 C:FN1302 4.8 48.1 1.0 NE D:ARG104 4.9 44.4 1.0 O D:LEU112 4.9 34.6 1.0 CB D:LEU112 4.9 36.5 1.0 HE2 C:TYR192 4.9 60.5 1.0 CG2 C:THR144 4.9 39.7 1.0 O C:TRP143 5.0 37.1 1.0

Fluorine binding site 4 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ D:F302 b:61.8 occ:1.00 F13 D:FN1302 0.0 61.8 1.0 C4 D:FN1302 1.3 58.7 1.0 C3 D:FN1302 2.3 58.5 1.0 C5 D:FN1302 2.5 53.9 1.0 H3 D:FN1302 2.5 70.2 1.0 HG3 E:ARG104 2.7 49.7 1.0 H5 D:FN1302 2.7 64.7 1.0 HG2 E:ARG104 3.1 49.7 1.0 CG E:ARG104 3.3 41.4 1.0 N1 D:FN1302 3.7 48.8 1.0 C2 D:FN1302 3.7 60.3 1.0 HB2 E:ARG104 3.9 47.2 1.0 HH D:TYR192 3.9 71.0 1.0 HA D:THR144 3.9 42.5 1.0 HG22 D:THR144 4.1 44.1 1.0 C1 D:FN1302 4.2 58.4 1.0 OH D:TYR192 4.2 59.2 1.0 CB E:ARG104 4.2 39.3 1.0 SG D:CYS188 4.3 92.7 1.0 HD3 E:ARG104 4.4 51.4 1.0 HB D:THR144 4.4 47.4 1.0 CD E:ARG104 4.4 42.9 1.0 O D:HOH402 4.6 49.9 1.0 O D:THR144 4.7 47.7 1.0 H6 D:FN1302 4.7 74.8 1.0 HB3 E:ARG104 4.7 47.2 1.0 CA D:THR144 4.8 35.4 1.0 CB E:LEU112 4.8 40.1 1.0 HE E:ARG104 4.8 50.6 1.0 H103 D:FN1302 4.8 81.5 1.0 H E:ARG104 4.9 43.1 1.0 C6 D:FN1302 4.9 62.3 1.0 O E:LEU112 4.9 40.1 1.0 CB D:THR144 4.9 39.5 1.0 CG2 D:THR144 4.9 36.8 1.0 HE1 E:MET114 5.0 64.4 1.0 NE E:ARG104 5.0 42.2 1.0

Fluorine binding site 5 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ E:F301 b:62.9 occ:1.00 F13 E:FN1301 0.0 62.9 1.0 C4 E:FN1301 1.3 61.2 1.0 C3 E:FN1301 2.3 66.3 1.0 C5 E:FN1301 2.5 57.3 1.0 H3 E:FN1301 2.5 79.6 1.0 H5 E:FN1301 2.7 68.8 1.0 HG3 A:ARG104 2.7 49.8 1.0 HG2 A:ARG104 3.3 49.8 1.0 HH E:TYR192 3.3 72.0 1.0 CG A:ARG104 3.4 41.5 1.0 HB2 A:ARG104 3.5 48.5 1.0 N1 E:FN1301 3.7 54.0 1.0 C2 E:FN1301 3.7 56.0 1.0 OH E:TYR192 3.8 60.0 1.0 SG E:CYS188 3.9 0.1 1.0 CB A:ARG104 4.0 40.4 1.0 HA E:THR144 4.1 40.5 1.0 C1 E:FN1301 4.1 51.4 1.0 HB3 A:ARG104 4.4 48.5 1.0 H27 E:FN1301 4.5 72.5 1.0 HB E:THR144 4.5 42.8 1.0 CD A:ARG104 4.6 42.5 1.0 H6 E:FN1301 4.7 70.0 1.0 O E:THR144 4.7 44.9 1.0 HD3 A:ARG104 4.7 51.0 1.0 HB3 E:CYS188 4.7 0.8 1.0 HE A:ARG104 4.8 53.2 1.0 HG22 E:THR144 4.8 52.7 1.0 C6 E:FN1301 4.8 58.3 1.0 CB A:LEU112 4.8 37.5 1.0 CA E:THR144 5.0 33.8 1.0 NE A:ARG104 5.0 44.3 1.0 CZ E:TYR192 5.0 63.4 1.0

Fluorine binding site 6 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ F:F301 b:70.7 occ:1.00 F13 F:FN1301 0.0 70.7 1.0 C4 F:FN1301 1.3 61.4 1.0 C3 F:FN1301 2.3 65.6 1.0 HG3 G:ARG104 2.3 50.8 1.0 C5 F:FN1301 2.5 55.5 1.0 H3 F:FN1301 2.5 78.7 1.0 HD23 G:LEU112 2.5 80.2 1.0 H5 F:FN1301 2.7 66.6 1.0 HG2 G:ARG104 3.0 50.8 1.0 CG G:ARG104 3.0 42.3 1.0 HB2 G:ARG104 3.4 49.5 1.0 CD2 G:LEU112 3.5 66.8 1.0 HH F:TYR192 3.6 70.9 1.0 N1 F:FN1301 3.7 60.0 1.0 C2 F:FN1301 3.7 63.9 1.0 CB G:ARG104 3.8 41.2 1.0 HD22 G:LEU112 3.8 80.2 1.0 HD21 G:LEU112 3.8 80.2 1.0 HB3 G:LEU112 3.9 64.4 1.0 HD11 G:LEU112 3.9 0.2 1.0 HA F:THR144 4.1 54.5 1.0 OH F:TYR192 4.1 59.1 1.0 C1 F:FN1301 4.1 57.9 1.0 CD G:ARG104 4.2 44.1 1.0 HB3 G:ARG104 4.3 49.5 1.0 HD3 G:ARG104 4.3 53.0 1.0 HG22 F:THR144 4.4 54.2 1.0 HE G:ARG104 4.4 51.1 1.0 CG G:LEU112 4.4 66.8 1.0 HB F:THR144 4.5 52.5 1.0 H6 F:FN1301 4.5 79.0 1.0 CD1 G:LEU112 4.6 83.5 1.0 NE G:ARG104 4.7 42.5 1.0 H G:ARG104 4.7 51.1 1.0 CB G:LEU112 4.7 53.7 1.0 O F:THR144 4.7 43.0 1.0 C6 F:FN1301 4.8 65.8 1.0 HD12 G:LEU112 4.8 0.2 1.0 CA F:THR144 4.9 45.4 1.0 O G:LEU112 5.0 43.8 1.0 HD2 G:ARG104 5.0 53.0 1.0

Fluorine binding site 7 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ H:F303 b:61.5 occ:1.00 F13 H:FN1303 0.0 61.5 1.0 C4 H:FN1303 1.3 59.2 1.0 C3 H:FN1303 2.3 57.8 1.0 HG3 I:ARG104 2.4 51.2 1.0 C5 H:FN1303 2.5 50.7 1.0 H3 H:FN1303 2.5 69.3 1.0 H5 H:FN1303 2.7 60.9 1.0 CG I:ARG104 3.2 42.7 1.0 HG2 I:ARG104 3.2 51.2 1.0 HB2 I:ARG104 3.3 43.9 1.0 C2 H:FN1303 3.7 58.0 1.0 N1 H:FN1303 3.7 55.3 1.0 HG H:CYS188 3.7 77.8 1.0 HH H:TYR192 3.8 64.8 1.0 CB I:ARG104 3.8 36.6 1.0 SG H:CYS188 4.0 64.8 1.0 C1 H:FN1303 4.2 50.6 1.0 OH H:TYR192 4.2 54.0 1.0 CB I:LEU112 4.3 37.5 1.0 HB3 I:ARG104 4.3 43.9 1.0 HA H:THR144 4.4 41.4 1.0 CD I:ARG104 4.4 41.8 1.0 HE3 I:MET114 4.4 92.0 1.0 HE I:ARG104 4.5 45.9 1.0 HD3 I:ARG104 4.6 50.2 1.0 H I:ARG104 4.6 43.0 1.0 H6 H:FN1303 4.6 62.4 1.0 HB H:THR144 4.6 54.1 1.0 NE I:ARG104 4.8 38.2 1.0 O I:LEU112 4.8 39.5 1.0 C6 H:FN1303 4.8 52.0 1.0 HG22 H:THR144 4.9 49.0 1.0

Fluorine binding site 8 out of 8 in the X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of X-Ray Crystal Structure of Lymnaea Stagnalis Acetylcholine Binding Protein (Ls-Achbp) in Complex with 5-Fluoronicotine (Ti-4650) within 5.0Å range: probe atom residue distance (Å) B Occ J:F303 b:71.8 occ:1.00 F13 J:FN1303 0.0 71.8 1.0 C4 J:FN1303 1.3 69.3 1.0 C3 J:FN1303 2.3 56.3 1.0 HG3 F:ARG104 2.5 50.6 1.0 C5 J:FN1303 2.5 62.4 1.0 H3 J:FN1303 2.5 67.5 1.0 H5 J:FN1303 2.7 74.9 1.0 HG2 F:ARG104 3.2 50.6 1.0 CG F:ARG104 3.2 42.2 1.0 OH J:TYR192 3.5 75.0 1.0 HH J:TYR192 3.6 90.0 1.0 C2 J:FN1303 3.7 66.4 1.0 N1 J:FN1303 3.7 61.4 1.0 HB2 F:ARG104 3.8 58.5 1.0 HA J:THR144 3.9 48.5 1.0 CB F:ARG104 4.1 48.8 1.0 C1 J:FN1303 4.2 58.5 1.0 CD F:ARG104 4.3 44.3 1.0 HD3 F:ARG104 4.3 53.1 1.0 O J:THR144 4.4 42.4 1.0 HB3 J:CYS188 4.4 1.0 1.0 HE F:ARG104 4.4 46.1 1.0 HB J:THR144 4.4 47.4 1.0 HG J:CYS188 4.5 0.7 1.0 H103 J:FN1303 4.5 82.2 1.0 NE F:ARG104 4.5 38.4 1.0 HB3 F:ARG104 4.5 58.5 1.0 H6 J:FN1303 4.6 86.1 1.0 CZ J:TYR192 4.6 71.4 1.0 HE2 J:TYR192 4.6 76.9 1.0 CA J:THR144 4.7 40.4 1.0 HG22 J:THR144 4.8 43.2 1.0 C6 J:FN1303 4.8 71.8 1.0 C J:THR144 5.0 40.8 1.0

J.Bobango, B.Sankaran, J.F.Park, J.Wu, T.T.Talley. Comparisons of Binding Affinities For Neuronal Nicotinic Receptors (Nnrs) and Achbps To Be Published.