Manganese in PDB 1a3w: Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+

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

The structure of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+, PDB code: 1a3w 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 (°)	109.400, 102.700, 110.900, 90.00, 112.30, 90.00
R / Rfree (%)	21.8 / 32.3

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

Potassium

(K)

2 atoms

The binding sites of Manganese atom in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+ (pdb code 1a3w). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+, PDB code: 1a3w:
Jump to Manganese binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1001 b:16.0 occ:1.00 O1 A:PGA1005 2.0 20.0 1.0 OE2 A:GLU242 2.1 76.7 1.0 O1P A:PGA1005 2.1 20.0 1.0 OD2 A:ASP266 2.3 36.8 1.0 C1 A:PGA1005 2.6 20.0 1.0 C2 A:PGA1005 2.7 20.0 1.0 CD A:GLU242 3.0 76.7 1.0 CG A:GLU242 3.1 76.7 1.0 P A:PGA1005 3.3 20.0 1.0 CG A:ASP266 3.3 36.8 1.0 CB A:ASP266 3.5 36.8 1.0 O4P A:PGA1005 3.7 20.0 1.0 O2P A:PGA1005 3.8 20.0 1.0 O2 A:PGA1005 3.9 20.0 1.0 OE1 A:GLU242 4.2 76.7 1.0 CE1 A:PHE214 4.2 69.8 1.0 CZ A:PHE214 4.3 69.8 1.0 N A:ASP266 4.4 26.7 1.0 CB A:GLU242 4.4 76.7 1.0 OD1 A:ASP266 4.4 36.8 1.0 OG A:SER213 4.5 20.9 1.0 CA A:ASP266 4.6 26.7 1.0 CB A:ALA263 4.6 39.6 1.0 CE A:LYS240 4.7 41.9 1.0 O3P A:PGA1005 4.8 20.0 1.0 CD1 A:PHE214 5.0 69.8 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1003 b:16.0 occ:1.00 O1 B:PGA1006 2.0 20.0 1.0 OE2 B:GLU242 2.0 21.0 1.0 O1P B:PGA1006 2.2 20.0 1.0 OD2 B:ASP266 2.3 41.5 1.0 C1 B:PGA1006 2.6 20.0 1.0 C2 B:PGA1006 2.7 20.0 1.0 CD B:GLU242 2.9 21.0 1.0 CG B:GLU242 3.1 21.0 1.0 CG B:ASP266 3.3 41.5 1.0 P B:PGA1006 3.4 20.0 1.0 CB B:ASP266 3.5 41.5 1.0 O4P B:PGA1006 3.8 20.0 1.0 O2 B:PGA1006 3.9 20.0 1.0 O2P B:PGA1006 4.0 20.0 1.0 OE1 B:GLU242 4.1 21.0 1.0 CE1 B:PHE214 4.1 13.4 1.0 CZ B:PHE214 4.2 13.4 1.0 OG B:SER213 4.4 9.8 1.0 CB B:GLU242 4.4 21.0 1.0 N B:ASP266 4.4 18.6 1.0 OD1 B:ASP266 4.4 41.5 1.0 CB B:ALA263 4.6 3.3 1.0 CA B:ASP266 4.6 18.6 1.0 CE B:LYS240 4.7 46.0 1.0 O3P B:PGA1006 4.9 20.0 1.0 CD1 B:PHE214 4.9 13.4 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