Chlorine in PDB 4txi: Construct of Mical-1 Containing the Monooxygenase and Calponin Homology Domains

The structure of Construct of Mical-1 Containing the Monooxygenase and Calponin Homology Domains, PDB code: 4txi was solved by S.S.Alqassim, L.M.Amzel, M.A.Bianchet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.14 / 2.31
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	71.924, 49.885, 95.852, 90.00, 97.03, 90.00
R / Rfree (%)	21.6 / 27.9

The binding sites of Chlorine atom in the Construct of Mical-1 Containing the Monooxygenase and Calponin Homology Domains (pdb code 4txi). 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 Construct of Mical-1 Containing the Monooxygenase and Calponin Homology Domains, PDB code: 4txi:

Chlorine binding site 1 out of 1 in the Construct of Mical-1 Containing the Monooxygenase and Calponin Homology Domains


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Construct of Mical-1 Containing the Monooxygenase and Calponin Homology Domains within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:49.6 occ:1.00 O A:HOH818 2.2 46.1 1.0 N A:PHE119 3.1 37.4 1.0 N A:CYS23 3.1 53.2 1.0 CB A:CYS23 3.3 54.4 1.0 CB A:LYS118 3.5 60.6 1.0 CA A:LYS118 3.7 53.5 1.0 CA A:CYS23 3.8 55.6 1.0 C A:LYS118 3.8 41.1 1.0 O A:PHE119 3.9 47.4 1.0 NH2 A:ARG158 3.9 39.0 1.0 CA A:PHE119 4.0 44.5 1.0 CD1 A:LEU22 4.0 57.3 1.0 CG A:LEU22 4.1 63.2 1.0 C A:LEU22 4.1 56.0 1.0 CA A:LEU22 4.1 59.4 1.0 CB A:PHE119 4.2 49.0 1.0 C A:PHE119 4.2 48.4 1.0 CB A:LEU22 4.7 46.8 1.0 CG A:LYS118 4.7 66.0 1.0 SG A:CYS23 4.8 47.4 1.0 O A:GLN21 4.8 43.1 1.0 CG A:PHE119 4.8 48.0 1.0 CE A:LYS118 4.9 49.4 1.0 N A:GLN24 4.9 57.3 1.0 CZ A:ARG158 4.9 44.9 1.0 C A:CYS23 4.9 58.8 1.0

S.S.Alqassim, M.Urquiza, E.Borgnia, M.Nagib, L.M.Amzel, M.A.Bianchet. Modulation of Mical Monooxygenase Activity By Its Calponin Homology Domain: Structural and Mechanistic Insights. Sci Rep V. 6 22176 2016.
ISSN: ESSN 2045-2322
PubMed: 26935886
DOI: 10.1038/SREP22176