Potassium in PDB 8b31: Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070

All present enzymatic activity of Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070:
2.7.7.9;

The structure of Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070, PDB code: 8b31 was solved by J.U.Laustsen, A.Kumpf, I.Bento, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.02 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.086, 78.593, 89.788, 90, 93.89, 90
R / Rfree (%)	19.6 / 22.6

The binding sites of Potassium atom in the Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070 (pdb code 8b31). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070, PDB code: 8b31:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070


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 Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070 within 5.0Å range: probe atom residue distance (Å) B Occ A:K313 b:47.3 occ:1.00 O A:HOH513 2.4 27.9 1.0 OE2 A:GLU45 2.5 24.5 1.0 O A:HOH617 2.8 32.4 1.0 O A:LYS95 3.0 24.9 1.0 HA A:LYS95 3.1 25.9 1.0 HG3 B:PRO26 3.2 29.1 1.0 HB3 A:ARG98 3.2 30.5 1.0 CD A:GLU45 3.5 22.4 1.0 HG2 A:LYS95 3.5 28.6 1.0 HB3 A:LYS95 3.6 26.4 1.0 CA A:LYS95 3.7 25.8 1.0 HB2 A:ARG98 3.7 31.2 1.0 HG2 A:ARG98 3.7 34.7 1.0 HD3 B:PRO26 3.7 29.1 1.0 C A:LYS95 3.8 25.8 1.0 OE1 A:GLU45 3.8 22.1 1.0 CB A:ARG98 3.8 29.8 1.0 HD3 A:ARG98 3.9 41.2 1.0 CB A:LYS95 4.0 27.0 1.0 HG21 A:THR41 4.0 28.2 1.0 O A:HOH466 4.0 37.8 1.0 O A:HOH450 4.0 26.0 1.0 CG B:PRO26 4.0 28.9 1.0 HG22 A:THR41 4.0 28.4 1.0 HB3 B:PRO26 4.1 29.4 1.0 CG A:ARG98 4.2 36.4 1.0 HG1 A:THR41 4.2 30.0 0.0 CG A:LYS95 4.2 28.8 1.0 CD B:PRO26 4.3 29.1 1.0 O A:HOH606 4.4 46.4 1.0 O A:HOH597 4.5 48.9 1.0 CG2 A:THR41 4.5 28.3 1.0 CD A:ARG98 4.5 41.5 1.0 CB B:PRO26 4.6 28.2 1.0 OG1 A:THR41 4.7 25.4 1.0 HG3 A:LYS95 4.7 29.8 1.0 HD2 B:PRO26 4.7 27.6 1.0 H A:ARG98 4.8 28.2 1.0 HG2 B:PRO26 4.8 27.8 1.0 O A:HOH600 4.8 46.0 1.0 HE3 A:LYS95 4.8 31.3 1.0 CG A:GLU45 4.8 22.6 1.0 HG2 A:GLU45 4.9 22.0 1.0 HB2 A:LYS95 4.9 27.5 1.0 H A:ALA99 5.0 29.1 1.0 HB2 B:PRO26 5.0 28.6 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070 within 5.0Å range: probe atom residue distance (Å) B Occ A:K314 b:87.7 occ:1.00 O A:HOH423 2.5 42.1 1.0 HO1 A:EDO308 2.5 30.0 0.0 O1 A:EDO308 2.9 21.8 0.2 O A:ALA211 3.1 23.7 1.0 O A:HOH578 3.2 39.8 1.0 H12 A:EDO308 3.4 35.3 0.5 HA A:ALA212 3.4 25.5 1.0 O A:HOH616 3.4 57.6 1.0 HE2 A:TYR177 3.6 36.0 1.0 HD2 A:TYR177 3.6 34.2 1.0 O A:HOH480 3.7 34.9 1.0 OD2 A:ASP141 3.8 34.1 1.0 HO1 A:EDO308 3.8 30.0 0.0 O A:HOH604 4.1 50.0 1.0 C A:ALA211 4.2 26.8 1.0 O A:HOH542 4.2 56.0 1.0 H A:GLY213 4.2 22.4 1.0 OD1 A:ASP141 4.2 31.9 1.0 C1 A:EDO308 4.2 36.4 0.5 CE2 A:TYR177 4.2 38.8 1.0 CA A:ALA212 4.2 25.8 1.0 HE2 A:PHE167 4.2 25.0 1.0 CD2 A:TYR177 4.3 34.1 1.0 C1 A:EDO308 4.3 22.4 0.2 H11 A:EDO308 4.3 34.9 0.5 CG A:ASP141 4.4 31.1 1.0 N A:GLY213 4.5 22.4 1.0 H11 A:EDO308 4.5 22.8 0.2 O1 A:EDO308 4.6 33.1 0.5 N A:ALA212 4.6 26.1 1.0 C A:ALA212 4.6 25.0 1.0 O A:HOH446 4.7 33.7 1.0 H12 A:EDO308 4.8 22.1 0.2 H21 A:EDO308 5.0 22.2 0.2

A.Kumpf, A.Maier, J.U.Laustsen, C.M.Jeffries, I.Bento, D.Tischler. Crystal Structure Determination of A Highly Active Udp-Glucose Pyrophosphorylase From Thermocrispum Agreste Dsm 44070 To Be Published.