Potassium in PDB 6nu5: Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine

All present enzymatic activity of Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine:
2.7.1.40;

The structure of Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine, PDB code: 6nu5 was solved by D.Srivastava, S.Nandi, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.98 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.000, 94.130, 109.260, 90.00, 95.61, 90.00
R / Rfree (%)	16.6 / 18.2

The structure of Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Potassium atom in the Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine (pdb code 6nu5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine, PDB code: 6nu5:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine


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 - S437Y in Complex with L-Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:K606 b:12.4 occ:1.00 OD1 A:ASP113 2.6 13.0 1.0 O A:THR114 2.7 11.0 1.0 OD1 A:ASN75 2.7 13.1 1.0 OG A:SER77 2.8 12.6 1.0 O A:HOH1055 2.8 18.2 1.0 O A:HOH904 2.8 11.7 1.0 OG A:SER243 3.6 10.9 1.0 C A:THR114 3.7 11.0 1.0 CG A:ASP113 3.7 10.9 1.0 CG A:ASN75 3.8 13.3 1.0 CB A:SER77 3.8 12.5 1.0 NZ A:LYS270 3.9 10.1 1.0 O A:ASP113 4.0 10.8 1.0 N A:SER77 4.0 10.8 1.0 CA A:LYS115 4.2 9.4 1.0 NH2 A:ARG73 4.2 14.7 1.0 N A:LYS115 4.3 10.3 1.0 C A:ASP113 4.3 10.8 1.0 O A:HOH955 4.3 29.2 1.0 ND2 A:ASN75 4.3 17.1 1.0 OE2 A:GLU118 4.4 16.0 1.0 O A:HOH784 4.5 12.9 1.0 O A:LYS115 4.5 12.4 1.0 CA A:SER77 4.5 12.8 1.0 CB A:ASP113 4.5 11.2 1.0 OD2 A:ASP113 4.5 11.6 1.0 N A:THR114 4.6 8.9 1.0 N A:PHE76 4.7 10.2 1.0 CA A:THR114 4.8 9.9 1.0 C A:LYS115 4.8 13.3 1.0 CB A:SER243 4.8 7.0 1.0 CB A:ASN75 4.9 12.6 1.0 CA A:ASN75 4.9 12.1 1.0 C A:PHE76 5.0 13.0 1.0 C A:ASN75 5.0 11.8 1.0

Potassium binding site 2 out of 2 in the Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Pyruvate Kinase M2 Mutant - S437Y in Complex with L-Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ B:K608 b:13.0 occ:1.00 OD1 B:ASP113 2.7 12.1 1.0 O B:THR114 2.7 12.6 1.0 OD1 B:ASN75 2.7 13.5 1.0 OG B:SER77 2.8 15.2 1.0 O B:HOH778 2.8 13.5 1.0 O B:HOH1078 2.9 15.8 1.0 C B:THR114 3.7 13.1 1.0 OG B:SER243 3.7 11.2 1.0 CG B:ASN75 3.7 12.8 1.0 CG B:ASP113 3.8 10.8 1.0 CB B:SER77 3.9 12.3 1.0 O B:ASP113 4.0 11.0 1.0 NZ B:LYS270 4.1 9.4 1.0 N B:SER77 4.1 12.1 1.0 CA B:LYS115 4.1 12.4 1.0 N B:LYS115 4.2 12.0 1.0 OE2 B:GLU118 4.2 18.6 1.0 NH2 B:ARG73 4.3 16.2 1.0 C B:ASP113 4.3 10.9 1.0 O B:HOH1048 4.3 26.0 1.0 ND2 B:ASN75 4.3 16.4 1.0 O B:LYS115 4.4 14.5 1.0 O B:HOH827 4.5 11.3 1.0 CA B:SER77 4.5 14.5 1.0 OD2 B:ASP113 4.6 12.2 1.0 CB B:ASP113 4.6 8.7 1.0 N B:THR114 4.6 12.2 1.0 N B:PHE76 4.7 11.4 1.0 C B:LYS115 4.7 13.7 1.0 CA B:THR114 4.7 14.0 1.0 CB B:SER243 4.8 9.3 1.0 CB B:ASN75 4.9 13.0 1.0 CA B:ASN75 4.9 11.2 1.0

D.Srivastava, S.Nandi, M.Dey. Mechanistic and Structural Insights Into Cysteine-Mediated Inhibition of Pyruvate Kinase Muscle Isoform 2. Biochemistry V. 58 3669 2019.
ISSN: ISSN 0006-2960
PubMed: 31386812
DOI: 10.1021/ACS.BIOCHEM.9B00349