Potassium in PDB 1a3x: Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+

All present enzymatic activity of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+:
2.7.1.40;

The structure of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+, PDB code: 1a3x was solved by M.S.Jurica, A.Mesecar, P.J.Heath, W.Shi, T.Nowak, B.L.Stoddard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 3.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.300, 106.400, 105.500, 90.00, 110.80, 90.00
R / Rfree (%)	22.7 / 34.1

The structure of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+ also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Potassium atom in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+ (pdb code 1a3x). 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 From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+, PDB code: 1a3x:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K1002 b:15.0 occ:1.00 OD1 A:ASN51 2.8 15.6 1.0 OD1 A:ASP84 2.8 4.8 1.0 O3P A:PGA1005 2.8 20.0 1.0 O A:THR85 2.9 5.9 1.0 OG A:SER213 3.2 17.8 1.0 NZ A:LYS240 3.4 19.5 1.0 OG A:SER53 3.4 7.2 1.0 O A:ASP84 3.5 4.8 1.0 CG A:ASP84 3.8 4.8 1.0 O4P A:PGA1005 3.9 20.0 1.0 CG A:ASN51 3.9 15.6 1.0 NH2 A:ARG49 4.0 8.7 1.0 C A:THR85 4.0 15.1 1.0 P A:PGA1005 4.1 20.0 1.0 CB A:SER213 4.3 17.8 1.0 C A:ASP84 4.4 2.5 1.0 OD2 A:ASP84 4.4 4.8 1.0 CA A:LYS86 4.4 7.6 1.0 CB A:SER53 4.5 7.2 1.0 ND2 A:ASN51 4.6 15.6 1.0 N A:LYS86 4.7 7.6 1.0 O2P A:PGA1005 4.7 20.0 1.0 CB A:ASP84 4.7 4.8 1.0 CE A:LYS240 4.8 19.5 1.0 N A:GLY87 4.9 8.6 1.0 CB A:ASN51 5.0 15.6 1.0

Potassium binding site 2 out of 2 in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+ within 5.0Å range: probe atom residue distance (Å) B Occ B:K1004 b:15.0 occ:1.00 OD1 B:ASN51 2.3 16.5 1.0 OD1 B:ASP84 2.9 11.1 1.0 O3P B:PGA1006 2.9 20.0 1.0 OG B:SER53 3.0 12.3 1.0 O B:THR85 3.0 20.8 1.0 O B:ASP84 3.5 11.1 1.0 CG B:ASN51 3.5 16.5 1.0 OG B:SER213 3.7 14.2 1.0 NZ B:LYS240 3.7 25.7 1.0 NH2 B:ARG49 3.9 2.0 1.0 CG B:ASP84 3.9 11.1 1.0 C B:THR85 4.1 13.9 1.0 CB B:SER53 4.1 12.3 1.0 P B:PGA1006 4.2 20.0 1.0 O4P B:PGA1006 4.2 20.0 1.0 ND2 B:ASN51 4.2 16.5 1.0 O2P B:PGA1006 4.4 20.0 1.0 CA B:LYS86 4.4 25.9 1.0 C B:ASP84 4.4 5.6 1.0 OD2 B:ASP84 4.6 11.1 1.0 CB B:ASN51 4.6 16.5 1.0 N B:LYS86 4.6 25.9 1.0 N B:SER53 4.7 6.6 1.0 CB B:SER213 4.7 14.2 1.0 CB B:ASP84 4.7 11.1 1.0 CA B:SER53 4.9 6.6 1.0 CA B:ASN51 4.9 22.2 1.0 N B:PHE52 4.9 31.8 1.0

M.S.Jurica, A.Mesecar, P.J.Heath, W.Shi, T.Nowak, B.L.Stoddard. The Allosteric Regulation of Pyruvate Kinase By Fructose-1,6-Bisphosphate. Structure V. 6 195 1998.
ISSN: ISSN 0969-2126
PubMed: 9519410
DOI: 10.1016/S0969-2126(98)00021-5