Potassium in PDB 3u81: Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase

All present enzymatic activity of Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase:
2.1.1.6;

The structure of Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase, PDB code: 3u81 was solved by A.Ehler, D.Schlatter, M.Stihle, J.Benz, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.81 / 1.13
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.384, 61.333, 104.686, 90.00, 90.00, 90.00
R / Rfree (%)	13.4 / 16

The binding sites of Potassium atom in the Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase (pdb code 3u81). 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 Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase, PDB code: 3u81:

Potassium binding site 1 out of 1 in the Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of A Sah-Bound Semi-Holo Form of Rat Catechol-O- Methyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:K223 b:20.4 occ:1.00 O A:PHE189 2.3 17.1 1.0 O A:HOH503 2.4 23.9 1.0 O A:SER186 2.4 15.8 1.0 O A:VAL183 2.5 13.0 1.0 O A:ARG184 2.7 17.4 1.0 O A:HOH371 2.8 20.0 1.0 HA A:ARG184 3.2 15.4 1.0 C A:ARG184 3.2 14.1 1.0 HG A:CYS191 3.3 16.0 1.0 H A:SER186 3.5 17.9 1.0 C A:PHE189 3.5 12.7 1.0 C A:SER186 3.5 15.3 1.0 HB2 A:PHE189 3.5 14.5 1.0 C A:VAL183 3.6 11.8 1.0 CA A:ARG184 3.6 12.9 1.0 H A:PHE189 3.6 15.2 1.0 N A:SER186 3.7 15.0 1.0 HA A:GLU190 3.9 15.9 0.6 HA A:GLU190 4.0 16.1 0.4 N A:GLY185 4.1 13.6 1.0 N A:ARG184 4.1 12.4 1.0 CA A:SER186 4.1 15.2 1.0 HB3 A:SER186 4.2 17.5 1.0 C A:GLY185 4.2 15.6 1.0 CA A:PHE189 4.2 11.7 1.0 CB A:PHE189 4.3 12.1 1.0 N A:PHE189 4.3 12.7 1.0 SG A:CYS191 4.3 13.3 1.0 HA A:SER187 4.3 21.8 1.0 N A:GLU190 4.5 12.4 1.0 O A:HOH229 4.5 36.6 1.0 N A:SER187 4.5 17.3 1.0 HB3 A:PHE189 4.5 14.5 1.0 H A:CYS191 4.5 14.8 1.0 CA A:GLY185 4.6 14.2 1.0 H A:GLY185 4.6 16.4 1.0 CA A:GLU190 4.7 13.2 0.6 CB A:SER186 4.7 14.6 1.0 CA A:GLU190 4.7 13.4 0.4 HA2 A:GLY185 4.7 17.1 1.0 HA A:VAL183 4.7 13.1 1.0 O A:HOH252 4.8 45.3 1.0 O A:GLY185 4.8 19.3 1.0 CA A:SER187 4.8 18.2 1.0 CA A:VAL183 4.8 10.9 1.0 HB2 A:CYS191 4.9 15.3 1.0 O A:HOH340 4.9 38.3 1.0 H A:ARG184 4.9 14.8 1.0 HA A:SER186 5.0 18.2 1.0 N A:CYS191 5.0 12.3 1.0

M.Ellermann, C.Lerner, G.Burgy, A.Ehler, C.Bissantz, R.Jakob-Roetne, R.Paulini, O.Allemann, H.Tissot, D.Grunstein, M.Stihle, F.Diederich, M.G.Rudolph. Catechol-O-Methyltransferase in Complex with Substituted 3'-Deoxyribose Bisubstrate Inhibitors. Acta Crystallogr.,Sect.D V. 68 253 2012.
ISSN: ISSN 0907-4449
PubMed: 22349227
DOI: 10.1107/S0907444912001138