Potassium in PDB 6b6u: Pyruvate Kinase M2 Mutant - S437Y

All present enzymatic activity of Pyruvate Kinase M2 Mutant - S437Y:
2.7.1.40;

The structure of Pyruvate Kinase M2 Mutant - S437Y, PDB code: 6b6u was solved by D.Srivastava, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.99 / 1.35
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.350, 93.610, 109.360, 90.00, 95.64, 90.00
R / Rfree (%)	13 / 14.9

The structure of Pyruvate Kinase M2 Mutant - S437Y also contains other interesting chemical elements:

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

The binding sites of Potassium atom in the Pyruvate Kinase M2 Mutant - S437Y (pdb code 6b6u). 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, PDB code: 6b6u:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Pyruvate Kinase M2 Mutant - S437Y


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:K603 b:10.4 occ:1.00 OD1 A:ASP113 2.6 10.6 1.0 OD1 A:ASN75 2.7 11.3 1.0 O A:THR114 2.7 8.9 1.0 OG A:SER77 2.8 11.5 1.0 O A:HOH1057 2.8 13.1 1.0 O A:HOH878 2.8 7.9 1.0 HG A:SER243 3.0 10.5 1.0 HA A:LYS115 3.4 11.3 0.4 HA A:LYS115 3.4 11.2 0.6 H A:SER77 3.4 11.5 1.0 HZ3 A:LYS270 3.6 11.1 1.0 C A:THR114 3.7 8.7 1.0 OG A:SER243 3.7 8.8 1.0 CG A:ASP113 3.7 9.4 1.0 HZ2 A:LYS270 3.7 11.1 1.0 CG A:ASN75 3.7 11.8 1.0 HH21 A:ARG73 3.8 14.6 1.0 HB2 A:SER77 3.8 12.3 1.0 CB A:SER77 3.8 10.3 1.0 HZ1 A:LYS270 3.9 11.1 1.0 NZ A:LYS270 3.9 9.2 1.0 O A:ASP113 4.0 8.8 1.0 HD21 A:ASN75 4.1 16.2 1.0 N A:SER77 4.1 9.6 1.0 HH22 A:ARG73 4.1 14.6 1.0 CA A:LYS115 4.2 9.4 0.4 NH2 A:ARG73 4.2 12.1 1.0 CA A:LYS115 4.2 9.3 0.6 HB3 A:ASP113 4.3 10.4 1.0 C A:ASP113 4.3 8.0 1.0 N A:LYS115 4.3 9.3 1.0 O A:HOH1062 4.3 18.7 1.0 ND2 A:ASN75 4.3 13.5 1.0 HA A:ASN75 4.3 11.9 1.0 H A:PHE76 4.4 10.8 1.0 OE2 A:GLU118 4.4 13.0 1.0 O A:HOH785 4.5 8.6 1.0 OD2 A:ASP113 4.5 9.9 1.0 CB A:ASP113 4.5 8.7 1.0 CA A:SER77 4.5 10.6 1.0 O A:LYS115 4.5 10.4 1.0 N A:THR114 4.6 8.0 1.0 HB3 A:SER77 4.6 12.3 1.0 N A:PHE76 4.7 9.0 1.0 CA A:THR114 4.8 7.9 1.0 HA A:SER77 4.8 12.7 1.0 C A:LYS115 4.8 9.3 1.0 CB A:SER243 4.8 8.4 1.0 CB A:ASN75 4.9 10.9 1.0 CA A:ASN75 4.9 9.9 1.0 H A:LYS115 5.0 11.1 0.6 H A:LYS115 5.0 11.1 0.4 HB3 A:SER243 5.0 10.1 1.0 HB2 A:SER243 5.0 10.1 1.0

Potassium binding site 2 out of 2 in the Pyruvate Kinase M2 Mutant - S437Y


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:K603 b:10.7 occ:1.00 OD1 B:ASP113 2.6 10.7 1.0 O B:THR114 2.7 9.6 1.0 OD1 B:ASN75 2.8 10.7 1.0 O B:HOH902 2.8 7.9 1.0 OG B:SER77 2.8 11.7 1.0 O B:HOH1098 2.8 13.4 1.0 HG B:SER243 3.0 11.6 1.0 HA B:LYS115 3.4 12.7 1.0 H B:SER77 3.5 12.8 1.0 HZ3 B:LYS270 3.6 11.0 1.0 C B:THR114 3.7 9.3 1.0 OG B:SER243 3.7 9.6 1.0 CG B:ASP113 3.7 9.5 1.0 CG B:ASN75 3.8 10.5 1.0 HH21 B:ARG73 3.9 13.7 1.0 HB2 B:SER77 3.9 12.7 1.0 HZ2 B:LYS270 3.9 11.0 1.0 CB B:SER77 3.9 10.6 1.0 O B:ASP113 4.0 8.6 1.0 HZ1 B:LYS270 4.0 11.0 1.0 NZ B:LYS270 4.0 9.2 1.0 HD21 B:ASN75 4.1 16.3 1.0 N B:SER77 4.1 10.7 1.0 CA B:LYS115 4.2 10.6 1.0 HH22 B:ARG73 4.2 13.7 1.0 N B:LYS115 4.2 9.9 1.0 HB3 B:ASP113 4.3 10.0 1.0 C B:ASP113 4.3 8.3 1.0 NH2 B:ARG73 4.3 11.4 1.0 HA B:ASN75 4.3 10.7 1.0 ND2 B:ASN75 4.4 13.6 1.0 OE2 B:GLU118 4.4 15.4 1.0 H B:PHE76 4.4 11.6 1.0 O B:LYS115 4.5 11.2 1.0 CB B:ASP113 4.5 8.3 1.0 OD2 B:ASP113 4.5 10.3 1.0 O B:HOH805 4.5 7.8 1.0 CA B:SER77 4.6 11.6 1.0 N B:THR114 4.6 8.7 1.0 HB3 B:SER77 4.7 12.7 1.0 C B:LYS115 4.7 10.8 1.0 CA B:THR114 4.7 9.2 1.0 N B:PHE76 4.7 9.6 1.0 HA B:SER77 4.8 13.9 1.0 CB B:SER243 4.8 9.4 1.0 CB B:ASN75 4.9 10.5 1.0 CA B:ASN75 4.9 8.9 1.0 HB2 B:SER243 5.0 11.2 1.0 H B:LYS115 5.0 11.9 1.0 HB3 B:SER243 5.0 11.2 1.0

D.Srivastava, M.Razzaghi, M.T.Henzl, M.Dey. Structural Investigation of A Dimeric Variant of Pyruvate Kinase Muscle Isoform 2. Biochemistry V. 56 6517 2017.
ISSN: ISSN 1520-4995
PubMed: 29182273
DOI: 10.1021/ACS.BIOCHEM.7B01013