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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1a3w:

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

Manganese (Mn) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium 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 Potassium atom.
In total 2 binding sites of Potassium where determined in the Pyruvate Kinase From Saccharomyces Cerevisiae Complexed with Fbp, Pg, MN2+ and K+, PDB code: 1a3w:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1a3w

Go back to Potassium Binding Sites List in 1a3w
Potassium 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 Potassium with other atoms in the K 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:K1002

b:16.0
occ:1.00
OD1 A:ASP84 2.7 13.4 1.0
OD1 A:ASN51 3.0 26.5 1.0
O A:THR85 3.0 59.8 1.0
O4P A:PGA1005 3.3 20.0 1.0
OG A:SER53 3.3 14.0 1.0
CG A:ASP84 3.6 13.4 1.0
O A:ASP84 3.8 13.4 1.0
O2P A:PGA1005 3.8 20.0 1.0
C A:THR85 3.9 62.7 1.0
CA A:LYS86 4.0 22.8 1.0
CG A:ASN51 4.0 26.5 1.0
CB A:SER53 4.1 14.0 1.0
CB A:ASP84 4.2 13.4 1.0
OG A:SER213 4.2 20.9 1.0
P A:PGA1005 4.2 20.0 1.0
N A:LYS86 4.3 22.8 1.0
C A:ASP84 4.3 28.7 1.0
NH1 A:ARG49 4.3 28.3 1.0
OD2 A:ASP84 4.5 13.4 1.0
N A:SER53 4.5 25.7 1.0
CB A:LYS86 4.6 34.9 1.0
CB A:SER213 4.7 20.9 1.0
CA A:SER53 4.7 25.7 1.0
NZ A:LYS240 4.8 41.9 1.0
CA A:ASN51 4.8 26.0 1.0
N A:PHE52 4.8 11.4 1.0
N A:THR85 4.8 62.7 1.0
CB A:ASN51 4.9 26.5 1.0
O3P A:PGA1005 4.9 20.0 1.0
CA A:ASP84 4.9 28.7 1.0
ND2 A:ASN51 4.9 26.5 1.0
CA A:THR85 5.0 62.7 1.0

Potassium binding site 2 out of 2 in 1a3w

Go back to Potassium Binding Sites List in 1a3w
Potassium 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 Potassium with other atoms in the K 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:K1004

b:16.0
occ:1.00
OD1 B:ASP84 2.7 19.9 1.0
O B:THR85 2.9 26.1 1.0
OD1 B:ASN51 3.0 18.8 1.0
O4P B:PGA1006 3.2 20.0 1.0
OG B:SER53 3.4 37.9 1.0
CG B:ASP84 3.6 19.9 1.0
O B:ASP84 3.7 19.9 1.0
O2P B:PGA1006 3.7 20.0 1.0
C B:THR85 3.7 5.8 1.0
CA B:LYS86 3.9 86.4 1.0
CG B:ASN51 4.1 18.8 1.0
CB B:ASP84 4.1 19.9 1.0
OG B:SER213 4.1 9.8 1.0
CB B:SER53 4.1 37.9 1.0
N B:LYS86 4.2 86.4 1.0
C B:ASP84 4.2 5.7 1.0
P B:PGA1006 4.2 20.0 1.0
NH1 B:ARG49 4.3 2.0 1.0
OD2 B:ASP84 4.5 19.9 1.0
N B:SER53 4.5 16.8 1.0
CB B:LYS86 4.5 41.0 1.0
CB B:SER213 4.6 9.8 1.0
NZ B:LYS240 4.7 46.0 1.0
N B:THR85 4.7 5.8 1.0
N B:PHE52 4.8 6.2 1.0
CA B:SER53 4.8 16.8 1.0
CA B:ASP84 4.8 5.7 1.0
CA B:ASN51 4.8 67.6 1.0
CA B:THR85 4.9 5.8 1.0
O3P B:PGA1006 4.9 20.0 1.0
CB B:ASN51 4.9 18.8 1.0
ND2 B:ASN51 5.0 18.8 1.0

Reference:

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
Page generated: Sun Dec 13 22:41:14 2020

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