Chlorine in PDB 1fmv: Crystal Structure of the Apo Motor Domain of Dictyostellium Myosin II

The structure of Crystal Structure of the Apo Motor Domain of Dictyostellium Myosin II, PDB code: 1fmv was solved by C.B.Bauer, H.M.Holden, J.B.Thoden, R.Smith, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.500, 179.700, 54.100, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Crystal Structure of the Apo Motor Domain of Dictyostellium Myosin II (pdb code 1fmv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Apo Motor Domain of Dictyostellium Myosin II, PDB code: 1fmv:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Apo Motor Domain of Dictyostellium Myosin II


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 the Apo Motor Domain of Dictyostellium Myosin II within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl800 b:31.4 occ:1.00 N A:TYR135 3.1 14.6 1.0 O A:HOH1094 3.3 33.6 1.0 CA A:PRO133 3.4 20.2 1.0 CB A:TYR135 3.5 15.1 1.0 C A:PRO133 3.5 35.4 1.0 CA A:TYR135 3.5 21.2 1.0 N A:ILE134 3.6 10.9 1.0 C A:TYR135 3.6 27.1 1.0 N A:THR136 3.6 23.4 1.0 CG2 A:THR136 3.8 27.5 1.0 CD2 A:TYR135 3.8 11.9 1.0 O A:ILE132 4.0 23.2 1.0 CG A:TYR135 4.1 28.9 1.0 O A:TYR135 4.2 28.5 1.0 C A:ILE134 4.2 13.5 1.0 O A:PRO133 4.2 16.7 1.0 O A:HOH1426 4.3 51.3 1.0 CB A:PRO133 4.3 26.9 1.0 CA A:THR136 4.5 25.8 1.0 CA A:ILE134 4.5 15.5 1.0 N A:PRO133 4.5 29.0 1.0 C A:ILE132 4.7 35.2 1.0 CB A:THR136 4.7 29.3 1.0

C.B.Bauer, H.M.Holden, J.B.Thoden, R.Smith, I.Rayment. X-Ray Structures of the Apo and Mgatp-Bound States of Dictyostelium Discoideum Myosin Motor Domain. J.Biol.Chem. V. 275 38494 2000.
ISSN: ISSN 0021-9258
PubMed: 10954715
DOI: 10.1074/JBC.M005585200