Phosphorus 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 binding sites of Phosphorus 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 Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Pg, MN2+ and K+, PDB code: 1a3x:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus 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 Phosphorus with other atoms in the P 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:P1005 b:20.0 occ:1.00 P A:PGA1005 0.0 20.0 1.0 O4P A:PGA1005 1.5 20.0 1.0 O1P A:PGA1005 1.5 20.0 1.0 O2P A:PGA1005 1.6 20.0 1.0 O3P A:PGA1005 1.7 20.0 1.0 C2 A:PGA1005 2.7 20.0 1.0 MN A:MN1001 2.9 15.0 1.0 NH2 A:ARG49 3.8 8.7 1.0 C1 A:PGA1005 3.9 20.0 1.0 K A:K1002 4.1 15.0 1.0 NZ A:LYS240 4.2 19.5 1.0 OD1 A:ASP266 4.3 14.8 1.0 O1 A:PGA1005 4.7 20.0 1.0 O2 A:PGA1005 4.7 20.0 1.0 CZ A:ARG49 4.9 8.7 1.0 OE1 A:GLU242 4.9 17.5 1.0 CE A:LYS240 5.0 19.5 1.0

Phosphorus 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 Phosphorus with other atoms in the P 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:P1006 b:20.0 occ:1.00 P B:PGA1006 0.0 20.0 1.0 O4P B:PGA1006 1.5 20.0 1.0 O1P B:PGA1006 1.6 20.0 1.0 O2P B:PGA1006 1.6 20.0 1.0 O3P B:PGA1006 1.7 20.0 1.0 MN B:MN1003 2.7 15.0 1.0 C2 B:PGA1006 2.7 20.0 1.0 OD1 B:ASP266 3.8 10.3 1.0 C1 B:PGA1006 4.0 20.0 1.0 NZ B:LYS240 4.1 25.7 1.0 K B:K1004 4.2 15.0 1.0 OE1 B:GLU242 4.3 16.6 1.0 NH2 B:ARG49 4.3 2.0 1.0 O1 B:PGA1006 4.5 20.0 1.0 OG B:SER213 4.7 14.2 1.0 CE B:LYS240 4.8 25.7 1.0 CG B:ASP266 5.0 10.3 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