Potassium in PDB 2qjf: Crystal Structure of Atp-Sulfurylase Domain of Human Paps Synthetase 1

All present enzymatic activity of Crystal Structure of Atp-Sulfurylase Domain of Human Paps Synthetase 1:
2.7.7.4;

The structure of Crystal Structure of Atp-Sulfurylase Domain of Human Paps Synthetase 1, PDB code: 2qjf was solved by N.Sekulic, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.100, 99.900, 75.900, 90.00, 113.00, 90.00
R / Rfree (%)	16.8 / 22.5

The binding sites of Potassium atom in the Crystal Structure of Atp-Sulfurylase Domain of Human Paps Synthetase 1 (pdb code 2qjf). 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 Atp-Sulfurylase Domain of Human Paps Synthetase 1, PDB code: 2qjf:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Atp-Sulfurylase Domain of Human Paps Synthetase 1


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 Atp-Sulfurylase Domain of Human Paps Synthetase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K1001 b:28.3 occ:1.00 N A:HIS314 3.4 35.4 1.0 N A:ASP374 3.5 34.3 1.0 CA A:THR313 3.7 31.5 1.0 CA A:GLY373 4.0 35.5 1.0 C A:THR313 4.0 33.2 1.0 CG A:ASP374 4.1 37.1 1.0 CB A:THR313 4.1 31.5 1.0 CB A:ASP374 4.2 34.6 1.0 OD2 A:ASP374 4.2 40.0 1.0 C A:GLY373 4.3 35.0 1.0 CB A:HIS314 4.4 38.8 1.0 OD1 A:ASP374 4.4 40.5 1.0 CA A:HIS314 4.5 38.2 1.0 CA A:ASP374 4.5 33.9 1.0 CG2 A:THR313 4.5 30.5 1.0 O A:ALA312 4.6 28.7 1.0 O A:HOH1064 4.6 33.1 1.0 N A:THR313 4.9 30.3 1.0 CD1 A:TRP375 4.9 34.5 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Atp-Sulfurylase Domain of Human Paps Synthetase 1


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 Atp-Sulfurylase Domain of Human Paps Synthetase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:K1002 b:44.7 occ:1.00 N B:ASP374 3.6 42.0 1.0 N B:HIS314 3.6 52.4 1.0 OD2 B:ASP374 3.7 50.0 1.0 CA B:THR313 3.8 49.0 1.0 CB B:ASP374 4.0 42.6 1.0 CG B:ASP374 4.1 45.5 1.0 CB B:THR313 4.1 48.9 1.0 C B:THR313 4.2 50.4 1.0 CA B:GLY373 4.2 42.7 1.0 C B:GLY373 4.4 42.4 1.0 CA B:ASP374 4.4 42.1 1.0 CG2 B:THR313 4.6 48.8 1.0 CB B:HIS314 4.7 55.0 1.0 CA B:HIS314 4.7 54.6 1.0 O B:ALA312 4.9 44.9 1.0

N.Sekulic, I.Paarmann, M.Konrad, A.Lavie. Atp-Sulfurylase Domain of Human Bifunctional Paps-Synthetase Oscillates Between Dimeric and Monomeric Forms To Be Published.