Chlorine in PDB 4pyn: Humanized Rat Comt in Complex with Sah

All present enzymatic activity of Humanized Rat Comt in Complex with Sah:
2.1.1.6;

The structure of Humanized Rat Comt in Complex with Sah, PDB code: 4pyn 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)	31.75 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.316, 61.248, 104.781, 90.00, 90.00, 90.00
R / Rfree (%)	12.7 / 15.4

The structure of Humanized Rat Comt in Complex with Sah also contains other interesting chemical elements:

Potassium

(K)

3 atoms

The binding sites of Chlorine atom in the Humanized Rat Comt in Complex with Sah (pdb code 4pyn). 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 Humanized Rat Comt in Complex with Sah, PDB code: 4pyn:

Chlorine binding site 1 out of 1 in the Humanized Rat Comt in Complex with Sah


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Humanized Rat Comt in Complex with Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:19.1 occ:1.00 H A:ASP221 2.5 10.2 1.0 H A:PHE222 2.5 9.3 1.0 HB2 A:ASP221 2.7 13.9 1.0 HA A:THR219 2.8 8.7 1.0 O A:HOH403 3.1 8.7 1.0 N A:ASP221 3.1 8.5 1.0 HB A:THR219 3.2 9.3 1.0 C A:THR219 3.2 7.5 1.0 N A:PHE222 3.3 7.7 1.0 CA A:THR219 3.4 7.2 1.0 HD2 A:PRO220 3.4 10.1 1.0 O A:HOH421 3.5 21.5 1.0 N A:PRO220 3.5 7.5 1.0 CB A:ASP221 3.5 11.6 1.0 O A:THR219 3.6 7.6 1.0 CA A:ASP221 3.7 9.7 1.0 CB A:THR219 3.8 7.8 1.0 HB3 A:PHE222 3.8 8.7 1.0 O A:HOH414 3.9 28.7 1.0 CD A:PRO220 3.9 8.4 1.0 HB2 A:PHE222 3.9 8.7 1.0 C A:ASP221 4.0 8.8 1.0 C A:PRO220 4.1 8.7 1.0 HG2 A:PRO220 4.1 11.5 1.0 CB A:PHE222 4.2 7.2 1.0 HG22 A:THR219 4.2 10.5 1.0 HB3 A:ASP221 4.3 13.9 1.0 CG A:ASP221 4.3 14.9 1.0 O A:LYS187 4.3 7.0 1.0 CA A:PRO220 4.4 8.2 1.0 CA A:PHE222 4.4 7.4 1.0 HA A:ASP188 4.5 9.0 1.0 CG A:PRO220 4.5 9.6 1.0 HB2 A:LEU191 4.6 9.6 1.0 CG2 A:THR219 4.6 8.7 1.0 OD2 A:ASP221 4.6 15.9 1.0 HB2 A:TYR190 4.6 7.2 1.0 HA A:ASP221 4.6 11.6 1.0 N A:THR219 4.7 7.5 1.0 H A:LEU191 4.7 7.6 1.0 HD3 A:PRO220 4.7 10.1 1.0 HB3 A:LEU191 4.8 9.6 1.0 HG1 A:THR219 4.8 9.2 1.0 HA A:PHE222 4.9 8.9 1.0 H A:LEU223 4.9 8.9 1.0 OG1 A:THR219 4.9 7.7 1.0 OD1 A:ASP221 5.0 16.1 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