Potassium in PDB 5l9w: Crystal Structure of the Apc Core Complex

All present enzymatic activity of Crystal Structure of the Apc Core Complex:
6.4.1.8;

The structure of Crystal Structure of the Apc Core Complex, PDB code: 5l9w was solved by E.Warkentin, S.Weidenweber, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.97 / 2.90
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	240.080, 240.080, 336.640, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 23.5

The structure of Crystal Structure of the Apc Core Complex also contains other interesting chemical elements:

Mercury

(Hg)

4 atoms

The binding sites of Potassium atom in the Crystal Structure of the Apc Core Complex (pdb code 5l9w). 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 the Apc Core Complex, PDB code: 5l9w:

Potassium binding site 1 out of 1 in the Crystal Structure of the Apc Core Complex


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 the Apc Core Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:K703 b:0.5 occ:1.00 OD1 A:ASP500 2.6 0.0 1.0 OD1 A:ASN501 2.6 93.3 1.0 OD2 A:ASP500 3.0 90.6 1.0 CG A:ASP500 3.2 91.0 1.0 OG1 A:THR365 3.2 95.0 1.0 CG2 A:THR365 3.5 79.4 1.0 CB A:THR365 3.7 81.8 1.0 O A:ASN394 3.7 93.4 1.0 CG A:ASN501 3.8 86.5 1.0 OG1 A:THR506 3.9 83.5 1.0 O A:MET362 4.0 97.8 1.0 O A:GLY395 4.1 83.1 1.0 CB A:THR506 4.5 79.0 1.0 ND2 A:ASN501 4.5 91.0 1.0 CB A:ASP500 4.7 80.4 1.0 C A:GLY395 4.9 75.1 1.0 CA A:GLY395 4.9 67.4 1.0 C A:ASN394 4.9 82.9 1.0 CB A:ASN501 4.9 76.7 1.0 N A:ASP500 4.9 92.6 1.0

S.Weidenweber, K.Schuhle, U.Demmer, E.Warkentin, U.Ermler, J.Heider. Structure of the Acetophenone Carboxylase Core Complex: Prototype of A New Class of Atp-Dependent Carboxylases/Hydrolases. Sci Rep V. 7 39674 2017.
ISSN: ESSN 2045-2322
PubMed: 28054554
DOI: 10.1038/SREP39674