Chlorine in PDB 4pyk: Human Comt, Double Domain Swap

All present enzymatic activity of Human Comt, Double Domain Swap:
2.1.1.6;

The structure of Human Comt, Double Domain Swap, PDB code: 4pyk was solved by A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.22 / 2.22
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	54.786, 66.825, 128.032, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 24.3

The structure of Human Comt, Double Domain Swap also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Human Comt, Double Domain Swap (pdb code 4pyk). 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 Human Comt, Double Domain Swap, PDB code: 4pyk:

Chlorine binding site 1 out of 1 in the Human Comt, Double Domain Swap


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Comt, Double Domain Swap within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:52.0 occ:1.00 O A:HOH444 3.2 41.6 1.0 N A:TYR121 3.3 40.5 1.0 N A:TYR118 3.3 48.4 1.0 N A:GLY120 3.3 45.2 1.0 N A:CYS119 3.5 50.9 1.0 N A:SER122 3.5 41.3 1.0 CB A:TYR118 3.7 52.4 1.0 CB A:TYR121 3.8 40.6 1.0 CA A:TYR118 3.9 49.0 1.0 C A:GLY120 3.9 45.8 1.0 OG A:SER122 3.9 48.9 1.0 CA A:GLY120 3.9 46.5 1.0 CA A:TYR121 4.0 41.9 1.0 C A:TYR118 4.1 53.6 1.0 CB A:SER122 4.2 37.6 1.0 SG A:CYS119 4.2 64.4 1.0 C A:CYS119 4.3 45.7 1.0 C A:TYR121 4.3 41.0 1.0 C A:ALA117 4.3 52.6 1.0 CA A:CYS119 4.4 50.0 1.0 CA A:ALA117 4.4 41.6 1.0 CA A:SER122 4.5 38.2 1.0 NH1 A:ARG251 4.8 58.5 1.0 O A:GLY120 4.9 40.7 1.0 CB A:CYS119 5.0 48.7 1.0 CG A:TYR118 5.0 63.5 1.0

A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph. Mapping the Conformational Space Accessible to Catechol-O-Methyltransferase. Acta Crystallogr.,Sect.D V. 70 2163 2014.
ISSN: ISSN 0907-4449
PubMed: 25084335
DOI: 10.1107/S1399004714012917