Potassium in PDB 4pym: Humanized Rat Apo-Comt Bound to Sulphate

All present enzymatic activity of Humanized Rat Apo-Comt Bound to Sulphate:
2.1.1.6;

The structure of Humanized Rat Apo-Comt Bound to Sulphate, PDB code: 4pym 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)	30.77 / 1.19
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.250, 61.550, 104.200, 90.00, 90.00, 90.00
R / Rfree (%)	13.7 / 17

The binding sites of Potassium atom in the Humanized Rat Apo-Comt Bound to Sulphate (pdb code 4pym). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Humanized Rat Apo-Comt Bound to Sulphate, PDB code: 4pym:

Potassium binding site 1 out of 1 in the Humanized Rat Apo-Comt Bound to Sulphate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Humanized Rat Apo-Comt Bound to Sulphate within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:17.9 occ:1.00 O A:PHE232 2.6 18.1 1.0 O A:SER229 2.6 17.9 1.0 O A:HOH591 2.8 43.0 1.0 O A:ARG227 2.8 17.7 1.0 O A:VAL226 2.8 14.6 1.0 O A:HOH423 2.9 21.4 1.0 HA A:ARG227 3.3 17.8 1.0 C A:ARG227 3.3 16.4 1.0 HG A:CYS234 3.5 19.3 1.0 H A:SER229 3.5 20.3 1.0 C A:SER229 3.6 17.3 1.0 C A:PHE232 3.7 15.9 1.0 N A:SER229 3.8 16.9 1.0 CA A:ARG227 3.8 14.9 1.0 HB2 A:PHE232 3.9 16.3 1.0 H A:PHE232 3.9 16.6 1.0 C A:VAL226 3.9 13.7 1.0 HA A:GLU233 4.1 18.1 0.5 HA A:GLU233 4.1 18.4 0.5 N A:GLY228 4.2 15.3 1.0 CA A:SER229 4.2 16.5 1.0 O A:HOH656 4.2 45.6 1.0 C A:GLY228 4.2 16.9 1.0 HA A:SER230 4.3 25.0 1.0 N A:ARG227 4.4 13.5 1.0 HB3 A:SER229 4.4 18.2 1.0 SG A:CYS234 4.5 16.1 1.0 CA A:PHE232 4.5 14.0 1.0 N A:PHE232 4.5 13.8 1.0 CB A:PHE232 4.6 13.6 1.0 H A:CYS234 4.6 17.9 1.0 N A:SER230 4.6 19.0 1.0 CA A:GLY228 4.6 15.9 1.0 HA2 A:GLY228 4.6 19.1 1.0 N A:GLU233 4.7 14.6 1.0 H A:GLY228 4.7 18.3 1.0 CA A:GLU233 4.8 15.1 0.5 CA A:GLU233 4.8 15.3 0.5 HB3 A:PHE232 4.9 16.3 1.0 CA A:SER230 4.9 20.8 1.0 O A:GLY228 4.9 20.5 1.0 CB A:SER229 4.9 15.2 1.0 HB2 A:CYS234 4.9 18.0 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