Potassium in PDB 4p7k: Rat Comt in Complex with Sinefungin

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

The structure of Rat Comt in Complex with Sinefungin, PDB code: 4p7k 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)	31.70 / 1.22
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.235, 61.238, 104.802, 90.00, 90.00, 90.00
R / Rfree (%)	11.2 / 14.8

The binding sites of Potassium atom in the Rat Comt in Complex with Sinefungin (pdb code 4p7k). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Rat Comt in Complex with Sinefungin, PDB code: 4p7k:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Rat Comt in Complex with Sinefungin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Rat Comt in Complex with Sinefungin within 5.0Å range: probe atom residue distance (Å) B Occ A:K302 b:26.0 occ:1.00 O A:SER101 2.4 15.7 1.0 O A:HOH614 2.6 23.0 1.0 OG A:SER103 3.1 17.3 1.0 HG A:SER103 3.3 20.8 1.0 O A:HOH401 3.5 38.5 1.0 H A:SER103 3.5 12.9 1.0 HG A:SER101 3.6 22.0 0.5 C A:SER101 3.6 13.6 1.0 N A:SER103 3.8 10.8 1.0 HA A:PRO102 3.8 12.2 1.0 O A:HOH534 3.8 36.5 1.0 HB3 A:SER101 3.9 19.7 0.5 HB2 A:SER101 4.1 14.9 0.5 C A:PRO102 4.1 10.6 1.0 CB A:SER103 4.1 13.7 1.0 HB2 A:SER103 4.2 16.4 1.0 CA A:PRO102 4.2 10.1 1.0 OG A:SER101 4.3 18.4 0.5 HB3 A:SER101 4.3 14.9 0.5 O A:HOH597 4.3 19.3 1.0 OE1 A:GLN124 4.3 18.9 0.5 O A:HOH415 4.3 32.7 1.0 CA A:SER103 4.4 10.9 1.0 N A:PRO102 4.4 11.9 1.0 CB A:SER101 4.4 16.4 0.5 HA A:SER103 4.5 13.1 1.0 CB A:SER101 4.5 12.4 0.5 O A:TYR100 4.6 12.1 1.0 CA A:SER101 4.7 14.2 0.5 CA A:SER101 4.7 12.9 0.5 O A:PRO102 4.8 12.2 1.0 HB3 A:SER103 5.0 16.4 1.0

Potassium binding site 2 out of 3 in the Rat Comt in Complex with Sinefungin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Rat Comt in Complex with Sinefungin within 5.0Å range: probe atom residue distance (Å) B Occ A:K303 b:17.7 occ:1.00 O A:HOH694 2.1 21.8 1.0 O A:HOH685 2.7 18.2 1.0 O A:HOH678 2.9 21.5 1.0 OH A:TYR190 2.9 7.4 1.0 O A:HIS185 2.9 9.7 1.0 OD1 A:ASP184 3.0 8.9 1.0 HA A:ASP184 3.2 7.0 1.0 OD1 A:ASN213 3.2 12.8 1.0 HH A:TYR190 3.3 8.9 1.0 O A:ASP184 3.3 8.8 1.0 C A:ASP184 3.3 7.2 1.0 HB2 A:ASN213 3.5 10.7 1.0 HE1 A:TYR190 3.6 8.0 1.0 HNE2 A:SFG300 3.7 14.3 1.0 N A:HIS185 3.7 6.2 1.0 CA A:ASP184 3.7 5.8 1.0 C A:HIS185 3.9 7.3 1.0 CZ A:TYR190 4.0 5.8 1.0 CG A:ASP184 4.0 7.7 1.0 HNE1 A:SFG300 4.0 14.3 1.0 CG A:ASN213 4.1 9.9 1.0 H A:HIS185 4.1 7.5 1.0 O A:HOH626 4.1 31.1 1.0 CE1 A:TYR190 4.2 6.7 1.0 CB A:ASN213 4.2 8.9 1.0 HA A:HIS185 4.3 8.1 1.0 CA A:HIS185 4.3 6.8 1.0 NE A:SFG300 4.3 11.9 1.0 H5'1 A:SFG300 4.4 8.9 1.0 O A:HOH653 4.5 29.0 1.0 CB A:ASP184 4.5 6.9 1.0 HB3 A:ASP212 4.5 9.0 1.0 O A:HOH606 4.5 18.7 1.0 O A:HOH675 4.6 29.8 1.0 HB3 A:ASN213 4.6 10.7 1.0 O A:ASP212 4.6 6.0 1.0 O A:HOH620 4.9 15.9 1.0 N A:ASP184 4.9 5.5 1.0 O A:HOH613 5.0 25.4 1.0 OD2 A:ASP184 5.0 8.3 1.0

Potassium binding site 3 out of 3 in the Rat Comt in Complex with Sinefungin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Rat Comt in Complex with Sinefungin within 5.0Å range: probe atom residue distance (Å) B Occ A:K304 b:14.3 occ:1.00 O A:PHE232 2.6 15.0 1.0 O A:SER229 2.6 13.4 1.0 O A:ARG227 2.8 14.6 1.0 O A:VAL226 2.8 10.2 1.0 O A:HOH599 2.9 17.9 1.0 HA A:ARG227 3.3 12.6 1.0 C A:ARG227 3.3 12.4 1.0 H A:SER229 3.6 16.0 1.0 C A:SER229 3.6 13.9 1.0 C A:PHE232 3.7 12.2 1.0 CA A:ARG227 3.8 10.5 1.0 N A:SER229 3.8 13.3 1.0 H A:PHE232 3.9 13.4 1.0 HB2 A:PHE232 3.9 12.3 1.0 C A:VAL226 3.9 9.6 1.0 HA A:GLU233 4.0 14.5 0.5 HA A:GLU233 4.1 14.9 0.5 N A:GLY228 4.2 11.7 1.0 HA A:SER230 4.2 19.9 1.0 CA A:SER229 4.3 13.1 1.0 C A:GLY228 4.3 13.7 1.0 N A:ARG227 4.4 10.0 1.0 SG A:CYS234 4.5 11.8 1.0 CA A:PHE232 4.5 10.8 1.0 HB3 A:SER229 4.5 14.9 1.0 H A:CYS234 4.5 13.7 1.0 N A:PHE232 4.6 11.2 1.0 CB A:PHE232 4.6 10.3 1.0 N A:SER230 4.6 14.9 1.0 CA A:GLY228 4.6 12.4 1.0 HA2 A:GLY228 4.7 14.9 1.0 N A:GLU233 4.7 11.6 1.0 H A:GLY228 4.8 14.1 1.0 CA A:GLU233 4.8 12.1 0.5 CA A:GLU233 4.8 12.4 0.5 CA A:SER230 4.8 16.6 1.0 HB3 A:PHE232 4.9 12.3 1.0 O A:GLY228 4.9 16.5 1.0 HB2 A:CYS234 5.0 13.8 1.0 CB A:SER229 5.0 12.4 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: ESSN 1399-0047
PubMed: 25084335
DOI: 10.1107/S1399004714012917