Chlorine in PDB 3wtk: Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid

The structure of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid, PDB code: 3wtk was solved by T.Okajima, M.Ihara, A.Yamashita, T.Oda, K.Matsuda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.60 / 2.69
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	74.534, 74.534, 350.816, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 27.4

The binding sites of Chlorine atom in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid (pdb code 3wtk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid, PDB code: 3wtk:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:29.4 occ:1.00 CL7 A:TH4301 0.0 29.4 1.0 C1 A:TH4301 1.8 35.9 1.0 C6 A:TH4301 2.7 39.0 1.0 N2 A:TH4301 2.7 36.5 1.0 O A:LEU112 2.8 33.7 1.0 O A:HOH433 3.1 25.8 1.0 N A:ARG104 3.6 36.4 1.0 C A:LEU112 3.6 34.4 1.0 CB A:ARG104 3.6 37.3 1.0 CG A:LEU112 3.7 39.8 1.0 O A:LEU102 3.9 35.1 1.0 C A:ALA103 3.9 37.1 1.0 CA A:TYR113 3.9 32.3 1.0 CG2 E:THR144 3.9 32.5 1.0 N A:MET114 4.0 29.8 1.0 CA A:ALA103 4.0 36.9 1.0 C3 A:TH4301 4.0 41.7 1.0 C5 A:TH4301 4.0 42.5 1.0 N A:TYR113 4.1 33.9 1.0 CA A:ARG104 4.2 37.4 1.0 CD2 A:LEU112 4.3 40.9 1.0 CB A:LEU112 4.4 37.0 1.0 C A:TYR113 4.4 31.0 1.0 C4 A:TH4301 4.6 45.3 1.0 CD1 A:LEU112 4.6 37.6 1.0 CA A:LEU112 4.7 35.9 1.0 CB E:THR144 4.7 30.9 1.0 O A:ALA103 4.7 37.0 1.0 C A:LEU102 4.7 35.9 1.0 CG A:ARG104 4.8 39.5 1.0 N A:ALA103 4.8 36.3 1.0 CB A:MET114 4.9 31.6 1.0

Chlorine binding site 2 out of 5 in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:37.7 occ:1.00 CL7 B:TH4301 0.0 37.7 1.0 C1 B:TH4301 1.8 42.7 1.0 N2 B:TH4301 2.7 45.0 1.0 C6 B:TH4301 2.8 44.1 1.0 O B:LEU112 2.9 30.5 1.0 C B:LEU112 3.5 32.5 1.0 N B:ARG104 3.5 32.0 1.0 N B:MET114 3.6 33.4 1.0 O B:HOH402 3.6 17.2 1.0 CA B:TYR113 3.6 30.9 1.0 CG B:LEU112 3.8 35.2 1.0 O B:LEU102 3.8 30.5 1.0 CA B:ALA103 3.9 32.7 1.0 N B:TYR113 3.9 31.4 1.0 CB B:ARG104 3.9 33.3 1.0 C3 B:TH4301 4.0 46.7 1.0 C B:ALA103 4.0 32.7 1.0 C B:TYR113 4.1 31.5 1.0 C5 B:TH4301 4.1 45.6 1.0 CG2 A:THR144 4.2 35.9 1.0 CA B:ARG104 4.4 32.2 1.0 CD2 B:LEU112 4.4 34.1 1.0 CB B:LEU112 4.4 34.7 1.0 C4 B:TH4301 4.6 47.8 1.0 CB B:MET114 4.6 37.0 1.0 CA B:MET114 4.6 34.4 1.0 CA B:LEU112 4.6 34.0 1.0 C B:LEU102 4.7 31.7 1.0 CD1 B:LEU112 4.7 34.6 1.0 N B:ALA103 4.7 30.7 1.0 CB B:ALA103 4.8 33.1 1.0 CD1 B:TYR113 4.8 31.8 1.0 CB B:TYR113 4.9 30.5 1.0

Chlorine binding site 3 out of 5 in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:35.7 occ:1.00 CL7 C:TH4301 0.0 35.7 1.0 C1 C:TH4301 1.8 42.6 1.0 C6 C:TH4301 2.7 45.7 1.0 N2 C:TH4301 2.7 43.9 1.0 O C:LEU112 2.9 41.8 1.0 O C:HOH402 3.3 17.8 1.0 C C:LEU112 3.5 43.0 1.0 CA C:TYR113 3.6 37.6 1.0 N C:ARG104 3.6 34.3 1.0 CB C:ARG104 3.6 35.7 1.0 CG C:LEU112 3.7 48.0 1.0 N C:MET114 3.7 37.3 1.0 N C:TYR113 3.8 40.2 1.0 O C:LEU102 3.9 32.6 1.0 C C:ALA103 3.9 34.4 1.0 CA C:ALA103 3.9 34.0 1.0 C3 C:TH4301 4.0 46.6 1.0 C5 C:TH4301 4.1 46.4 1.0 C C:TYR113 4.1 38.3 1.0 CA C:ARG104 4.3 35.2 1.0 CD2 C:LEU112 4.3 49.0 1.0 CB C:LEU112 4.3 46.9 1.0 CG2 B:THR144 4.4 26.6 1.0 CA C:LEU112 4.6 44.6 1.0 C4 C:TH4301 4.6 48.9 1.0 CD1 C:LEU112 4.6 48.5 1.0 O C:ALA103 4.6 34.0 1.0 C C:LEU102 4.7 32.6 1.0 CG C:ARG104 4.7 35.1 1.0 N C:ALA103 4.8 33.1 1.0 CB C:TYR113 4.8 34.8 1.0 CA C:MET114 4.8 37.5 1.0 CB C:MET114 4.8 41.9 1.0 CD1 C:TYR113 4.9 34.6 1.0 CB C:ALA103 4.9 33.1 1.0

Chlorine binding site 4 out of 5 in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl301 b:26.8 occ:1.00 CL7 D:TH4301 0.0 26.8 1.0 C1 D:TH4301 1.8 31.2 1.0 O D:LEU112 2.7 33.3 1.0 N2 D:TH4301 2.7 34.1 1.0 C6 D:TH4301 2.8 32.1 1.0 C D:LEU112 3.4 32.7 1.0 CB D:ARG104 3.5 32.9 1.0 O D:HOH401 3.5 11.1 1.0 N D:ARG104 3.6 33.1 1.0 CA D:TYR113 3.6 32.4 1.0 N D:MET114 3.7 34.7 1.0 N D:TYR113 3.8 31.7 1.0 C D:ALA103 3.9 32.1 1.0 CA D:ALA103 4.0 32.7 1.0 CG D:LEU112 4.0 42.6 1.0 C3 D:TH4301 4.0 34.4 1.0 O D:LEU102 4.0 31.2 1.0 C5 D:TH4301 4.1 33.2 1.0 C D:TYR113 4.1 33.3 1.0 CA D:ARG104 4.2 33.3 1.0 CB D:LEU112 4.3 36.8 1.0 CG2 C:THR144 4.4 28.4 1.0 CA D:LEU112 4.4 33.0 1.0 C4 D:TH4301 4.6 36.1 1.0 O D:ALA103 4.6 29.8 1.0 CG D:ARG104 4.6 33.5 1.0 CB D:MET114 4.7 40.3 1.0 CA D:MET114 4.8 36.9 1.0 CD2 D:LEU112 4.8 43.5 1.0 C D:LEU102 4.9 33.0 1.0 CB D:TYR113 4.9 31.6 1.0 N D:ALA103 4.9 33.8 1.0 CD1 D:LEU112 4.9 44.8 1.0 CD1 D:TYR113 4.9 28.3 1.0 CB D:ALA103 5.0 30.7 1.0

Chlorine binding site 5 out of 5 in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Thiacloprid within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl301 b:27.6 occ:1.00 CL7 E:TH4301 0.0 27.6 1.0 C1 E:TH4301 1.8 33.5 1.0 C6 E:TH4301 2.7 37.6 1.0 N2 E:TH4301 2.8 37.0 1.0 O E:LEU112 2.8 33.0 1.0 O E:HOH401 3.3 7.3 1.0 N E:ARG104 3.3 37.1 1.0 CB E:ARG104 3.5 40.3 1.0 C E:LEU112 3.6 32.9 1.0 CA E:TYR113 3.7 29.0 1.0 N E:MET114 3.8 28.4 1.0 O E:LEU102 3.8 31.6 1.0 C E:ALA103 3.9 35.7 1.0 CA E:ALA103 3.9 34.0 1.0 N E:TYR113 4.0 30.0 1.0 CG2 D:THR144 4.0 29.0 1.0 C3 E:TH4301 4.0 38.0 1.0 CA E:ARG104 4.0 38.2 1.0 C5 E:TH4301 4.0 40.5 1.0 CG E:LEU112 4.1 41.0 1.0 C E:TYR113 4.3 29.2 1.0 CD2 E:LEU112 4.3 41.5 1.0 CB E:LEU112 4.5 37.1 1.0 C E:LEU102 4.6 31.5 1.0 C4 E:TH4301 4.6 42.4 1.0 CG E:ARG104 4.6 44.0 1.0 CA E:LEU112 4.6 34.3 1.0 N E:ALA103 4.7 32.3 1.0 CB E:MET114 4.8 29.1 1.0 CB D:THR144 4.8 32.6 1.0 CA E:MET114 4.9 28.8 1.0 CD1 E:TYR113 4.9 26.3 1.0 CB E:TYR113 4.9 27.8 1.0 O E:ALA103 4.9 36.2 1.0

M.Ihara, T.Okajima, A.Yamashita, T.Oda, T.Asano, M.Matsui, D.B.Sattelle, K.Matsuda. Studies on An Acetylcholine Binding Protein Identify A Basic Residue in Loop G on the Beta 1 Strand As A New Structural Determinant of Neonicotinoid Actions Mol.Pharmacol. V. 86 736 2014.
ISSN: ISSN 0026-895X
PubMed: 25267717
DOI: 10.1124/MOL.114.094698