Potassium in PDB 6wp3: Pyruvate Kinase M2 Mutant-K433Q

All present enzymatic activity of Pyruvate Kinase M2 Mutant-K433Q:
2.7.1.40;

The structure of Pyruvate Kinase M2 Mutant-K433Q, PDB code: 6wp3 was solved by S.Nandi, M.Razzaghi, D.Srivastava, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.11 / 1.84
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	112.378, 94.226, 109.638, 90.00, 94.80, 90.00
R / Rfree (%)	20.3 / 23

The structure of Pyruvate Kinase M2 Mutant-K433Q also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Potassium atom in the Pyruvate Kinase M2 Mutant-K433Q (pdb code 6wp3). 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 Pyruvate Kinase M2 Mutant-K433Q, PDB code: 6wp3:

Potassium binding site 1 out of 1 in the Pyruvate Kinase M2 Mutant-K433Q


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Pyruvate Kinase M2 Mutant-K433Q within 5.0Å range: probe atom residue distance (Å) B Occ B:K607 b:50.6 occ:1.00 OG1 B:THR87 3.0 35.3 1.0 CE2 B:TYR83 3.2 41.2 1.0 ND1 B:HIS84 3.6 39.0 1.0 O B:HOH725 3.7 30.2 1.0 O B:ILE51 3.7 29.0 1.0 CD2 B:TYR83 3.8 44.1 1.0 CB B:THR87 3.8 33.1 1.0 CG2 B:THR87 3.8 34.6 1.0 CE1 B:HIS84 4.0 38.8 1.0 CZ B:TYR83 4.0 40.7 1.0 CA B:GLY52 4.2 28.0 1.0 C B:ILE51 4.2 26.4 1.0 OH B:TYR83 4.2 40.4 1.0 NE B:ARG56 4.3 34.1 1.0 N B:GLY52 4.4 26.0 1.0 O B:TYR83 4.8 35.9 1.0 CD B:ARG56 4.9 34.6 1.0 C B:GLY52 4.9 27.4 1.0 CB B:ILE51 4.9 25.8 1.0 CG B:HIS84 4.9 37.7 1.0 CG2 B:ILE51 5.0 27.1 1.0 CA B:HIS84 5.0 36.7 1.0 CG B:TYR83 5.0 38.8 1.0

S.Nandi, M.Razzaghi, D.Srivastava, M.Dey. Structural Basis For Allosteric Regulation of Pyruvate Kinase M2 By Phosphorylation and Acetylation. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 32989054
DOI: 10.1074/JBC.RA120.015800