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

The structure of Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Clothianidin, PDB code: 3wti 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 / 2.68
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	74.145, 74.145, 351.612, 90.00, 90.00, 120.00
R / Rfree (%)	22.5 / 29.4

The binding sites of Chlorine atom in the Crystal Structure of Lymnaea Stagnalis Acetylcholine-Binding Protein Q55R Mutant Complexed with Clothianidin (pdb code 3wti). 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 Clothianidin, PDB code: 3wti:
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 Clothianidin


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 Clothianidin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:52.0 occ:1.00 CL A:CT4301 0.0 52.0 1.0 C4 A:CT4301 1.7 50.8 1.0 N4 A:CT4301 2.6 48.7 1.0 O B:LEU112 2.9 34.5 1.0 S A:CT4301 3.0 52.7 1.0 O B:HOH434 3.0 38.4 1.0 C B:LEU112 3.6 34.6 1.0 N B:MET114 3.7 31.5 1.0 CB B:ARG104 3.7 37.4 1.0 N B:ARG104 3.7 35.2 1.0 CA B:TYR113 3.8 32.2 1.0 C5 A:CT4301 3.8 48.5 1.0 CG B:LEU112 3.9 37.1 1.0 N B:TYR113 4.0 33.6 1.0 C2 A:CT4301 4.1 50.4 1.0 O B:LEU102 4.1 31.2 1.0 CG2 A:THR144 4.1 44.8 1.0 C B:ALA103 4.2 34.3 1.0 C B:TYR113 4.2 31.7 1.0 CA B:ALA103 4.3 32.8 1.0 CA B:ARG104 4.3 36.8 1.0 CB B:LEU112 4.5 37.6 1.0 CB B:MET114 4.6 32.5 1.0 CD1 B:LEU112 4.6 36.6 1.0 CD2 B:LEU112 4.6 38.8 1.0 CA B:MET114 4.7 31.3 1.0 CA B:LEU112 4.7 36.3 1.0 CG B:ARG104 4.9 39.4 1.0 CB A:THR144 4.9 45.8 1.0 C B:LEU102 5.0 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 Clothianidin


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 Clothianidin within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:42.8 occ:1.00 CL B:CT4301 0.0 42.8 1.0 C4 B:CT4301 1.7 43.0 1.0 N4 B:CT4301 2.6 41.9 1.0 S B:CT4301 3.0 44.9 1.0 O C:HOH426 3.1 33.1 1.0 O C:LEU112 3.1 35.6 1.0 N C:ARG104 3.3 36.3 1.0 O C:LEU102 3.5 32.6 1.0 CB C:ARG104 3.6 39.9 1.0 CA C:ALA103 3.7 33.3 1.0 C C:ALA103 3.7 35.1 1.0 C5 B:CT4301 3.8 42.6 1.0 C C:LEU112 3.9 35.9 1.0 CA C:TYR113 4.0 33.2 1.0 CG2 B:THR144 4.0 38.2 1.0 C2 B:CT4301 4.1 44.2 1.0 N C:MET114 4.1 33.3 1.0 CA C:ARG104 4.1 38.4 1.0 CG C:LEU112 4.3 40.0 1.0 N C:TYR113 4.3 34.8 1.0 C C:LEU102 4.3 32.4 1.0 N C:ALA103 4.4 32.6 1.0 C C:TYR113 4.6 33.2 1.0 O C:ALA103 4.6 35.6 1.0 CB B:THR144 4.7 39.1 1.0 CB C:ALA103 4.7 32.7 1.0 CB C:LEU112 4.8 40.0 1.0 CG C:ARG104 4.8 42.4 1.0 CD2 C:LEU112 4.9 42.6 1.0 CA C:LEU112 5.0 37.9 1.0 CD1 C:TYR113 5.0 30.4 1.0

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


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 Clothianidin within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:48.3 occ:1.00 CL C:CT4301 0.0 48.3 1.0 C4 C:CT4301 1.7 47.3 1.0 N4 C:CT4301 2.6 45.4 1.0 O D:LEU112 2.8 31.0 1.0 S C:CT4301 3.0 49.5 1.0 O C:HOH413 3.4 42.9 1.0 CB D:ARG104 3.5 33.8 1.0 C D:LEU112 3.6 31.2 1.0 CG D:LEU112 3.7 34.6 1.0 C5 C:CT4301 3.8 45.5 1.0 N D:ARG104 3.8 31.1 1.0 N D:MET114 4.0 29.6 1.0 CA D:TYR113 4.1 29.2 1.0 C2 C:CT4301 4.1 47.6 1.0 N D:TYR113 4.2 30.3 1.0 CB D:LEU112 4.2 34.3 1.0 C D:ALA103 4.2 30.2 1.0 CA D:ARG104 4.3 32.6 1.0 CD2 D:LEU112 4.3 36.8 1.0 O D:LEU102 4.4 28.8 1.0 C D:TYR113 4.4 29.4 1.0 CA D:ALA103 4.4 28.9 1.0 CG2 C:THR144 4.5 40.5 1.0 CA D:LEU112 4.5 32.6 1.0 CG D:ARG104 4.5 35.8 1.0 CB D:MET114 4.6 31.8 1.0 CD1 D:LEU112 4.8 34.4 1.0 CA D:MET114 4.9 30.1 1.0 O D:ALA103 4.9 30.6 1.0

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


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 Clothianidin within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl301 b:38.4 occ:1.00 CL D:CT4301 0.0 38.4 1.0 C4 D:CT4301 1.7 38.4 1.0 N4 D:CT4301 2.6 38.4 1.0 S D:CT4301 3.0 38.4 1.0 O E:LEU112 3.1 31.7 1.0 O E:HOH402 3.2 36.4 1.0 CB E:ARG104 3.6 35.5 1.0 CG E:LEU112 3.7 34.0 1.0 C5 D:CT4301 3.8 38.4 1.0 C E:LEU112 3.8 31.6 1.0 N E:MET114 3.9 28.8 1.0 CD2 E:LEU112 3.9 35.7 1.0 N E:ARG104 4.0 33.1 1.0 C2 D:CT4301 4.1 38.4 1.0 CA E:TYR113 4.1 29.2 1.0 O E:LEU102 4.3 30.2 1.0 N E:TYR113 4.3 30.4 1.0 C E:ALA103 4.4 32.5 1.0 CG2 D:THR144 4.4 34.9 1.0 CA E:ARG104 4.5 34.9 1.0 CB E:LEU112 4.5 34.4 1.0 C E:TYR113 4.5 28.6 1.0 CA E:ALA103 4.5 30.9 1.0 CB E:MET114 4.6 29.9 1.0 CG E:ARG104 4.7 37.6 1.0 CD1 E:LEU112 4.7 33.6 1.0 CA E:LEU112 4.8 33.0 1.0 CA E:MET114 4.8 28.6 1.0 CB D:THR144 5.0 36.0 1.0

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


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 Clothianidin within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl301 b:41.7 occ:1.00 CL E:CT4301 0.0 41.7 1.0 C4 E:CT4301 1.7 40.7 1.0 N4 E:CT4301 2.6 38.8 1.0 O A:LEU112 2.9 31.2 1.0 S E:CT4301 3.0 42.6 1.0 O A:HOH428 3.1 27.9 1.0 CB A:ARG104 3.7 33.4 1.0 C A:LEU112 3.7 31.6 1.0 N A:ARG104 3.7 31.4 1.0 CG A:LEU112 3.8 33.7 1.0 C5 E:CT4301 3.8 38.6 1.0 N A:MET114 4.0 28.4 1.0 CA A:TYR113 4.0 29.4 1.0 C2 E:CT4301 4.1 40.5 1.0 O A:LEU102 4.1 28.1 1.0 CG2 E:THR144 4.2 35.8 1.0 N A:TYR113 4.2 30.8 1.0 CD2 A:LEU112 4.3 35.0 1.0 C A:ALA103 4.3 30.5 1.0 CA A:ARG104 4.4 32.8 1.0 C A:TYR113 4.4 28.9 1.0 CA A:ALA103 4.4 29.4 1.0 CB A:LEU112 4.5 34.3 1.0 CD1 A:LEU112 4.7 33.5 1.0 CA A:LEU112 4.8 33.4 1.0 CB A:MET114 4.8 29.2 1.0 CB E:THR144 4.8 36.5 1.0 CG A:ARG104 4.8 34.9 1.0 CA A:MET114 4.9 28.1 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