Potassium in PDB 6eji: Structure of A Glycosyltransferase

The structure of Structure of A Glycosyltransferase, PDB code: 6eji was solved by A.S.Ramirez, J.Boilevin, A.R.Mehdipour, G.Hummer, T.Darbre, J.L.Reymond, K.P.Locher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.94 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.620, 127.030, 71.580, 90.00, 90.13, 90.00
R / Rfree (%)	19.6 / 22.3

The structure of Structure of A Glycosyltransferase also contains other interesting chemical elements:

Chlorine	(Cl)	3 atoms
Sodium	(Na)	4 atoms

The binding sites of Potassium atom in the Structure of A Glycosyltransferase (pdb code 6eji). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of A Glycosyltransferase, PDB code: 6eji:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of A Glycosyltransferase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A Glycosyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:44.9 occ:1.00 NE A:ARG246 3.0 51.2 1.0 O A:HOH536 3.4 45.3 1.0 CL A:CL407 3.5 79.2 1.0 N A:ASP223 3.5 34.5 1.0 NH2 A:ARG246 3.5 44.1 1.0 CZ A:ARG246 3.6 47.2 1.0 CA A:GLY222 3.8 32.2 1.0 O A:ASP223 3.9 37.0 1.0 CD A:ARG246 3.9 47.2 1.0 CG A:ARG246 3.9 44.7 1.0 OG A:SER14 4.0 45.7 1.0 C5 A:UD2401 4.1 34.0 1.0 C A:GLY222 4.1 39.2 1.0 CA A:ARG191 4.1 37.5 1.0 N A:ARG191 4.2 36.6 1.0 C6 A:UD2401 4.5 34.8 1.0 C A:GLY190 4.5 33.6 1.0 CA A:ASP223 4.5 39.0 1.0 CB A:ARG246 4.6 39.1 1.0 O A:GLY190 4.6 33.0 1.0 C A:ASP223 4.6 40.6 1.0 CB A:ARG191 4.6 32.8 1.0 O A:HOH566 4.7 42.5 1.0 C4 A:UD2401 4.8 35.9 1.0 NH1 A:ARG246 4.9 45.8 1.0 CB A:ASP223 4.9 47.0 1.0

Potassium binding site 2 out of 2 in the Structure of A Glycosyltransferase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of A Glycosyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:K402 b:34.2 occ:1.00 CL B:CL406 3.3 72.4 1.0 N B:ASP223 3.7 37.1 1.0 OG B:SER14 3.8 36.7 1.0 CA B:GLY222 3.9 33.7 1.0 CG B:ARG246 3.9 38.2 1.0 C5 B:UD2401 4.0 32.7 1.0 CD B:ARG246 4.1 39.0 1.0 O B:ASP223 4.1 39.7 1.0 O B:HOH577 4.1 47.5 1.0 C B:GLY222 4.3 36.5 1.0 CA B:ARG191 4.3 35.7 1.0 N B:ARG191 4.4 39.5 1.0 C6 B:UD2401 4.4 32.4 1.0 C4 B:UD2401 4.5 34.7 1.0 CB B:ARG246 4.5 38.1 1.0 CB B:SER14 4.6 32.7 1.0 O4 B:UD2401 4.7 33.4 1.0 C B:GLY190 4.7 35.4 1.0 O B:HOH576 4.7 37.8 1.0 CA B:ASP223 4.8 38.6 1.0 CB B:ARG191 4.8 30.4 1.0 O B:GLY190 4.8 36.2 1.0 C B:ASP223 4.8 39.1 1.0

A.S.Ramirez, J.Boilevin, A.R.Mehdipour, G.Hummer, T.Darbre, J.L.Reymond, K.P.Locher. Structural Basis of the Molecular Ruler Mechanism of A Bacterial Glycosyltransferase. Nat Commun V. 9 445 2018.
ISSN: ESSN 2041-1723
PubMed: 29386647
DOI: 10.1038/S41467-018-02880-2