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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1a3x:

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

Potassium (K) 2 atoms

Manganese Binding Sites:

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

Manganese binding site 1 out of 2 in 1a3x

Go back to Manganese Binding Sites List in 1a3x
Manganese 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 Manganese with other atoms in the Mn 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:Mn1001

b:15.0
occ:1.00
OD1 A:ASP266 2.0 14.8 1.0
O4P A:PGA1005 2.2 20.0 1.0
OE1 A:GLU242 2.3 17.5 1.0
O1P A:PGA1005 2.3 20.0 1.0
P A:PGA1005 2.9 20.0 1.0
CG A:ASP266 3.0 14.8 1.0
CD A:GLU242 3.4 17.5 1.0
C2 A:PGA1005 3.4 20.0 1.0
C1 A:PGA1005 3.7 20.0 1.0
OD2 A:ASP266 3.8 14.8 1.0
OE2 A:GLU242 3.8 17.5 1.0
O3P A:PGA1005 3.8 20.0 1.0
O2 A:PGA1005 3.8 20.0 1.0
CB A:ASP266 3.9 14.8 1.0
N A:ASP266 4.0 13.4 1.0
O2P A:PGA1005 4.2 20.0 1.0
CZ A:PHE214 4.3 5.8 1.0
O1 A:PGA1005 4.5 20.0 1.0
CA A:ASP266 4.6 13.4 1.0
CE1 A:PHE214 4.6 5.8 1.0
CG A:GLU242 4.7 17.5 1.0
CB A:ALA263 4.8 8.0 1.0
CB A:GLU242 4.8 17.5 1.0
OG A:SER213 4.8 17.8 1.0
CE2 A:PHE214 4.9 5.8 1.0
NZ A:LYS240 5.0 19.5 1.0

Manganese binding site 2 out of 2 in 1a3x

Go back to Manganese Binding Sites List in 1a3x
Manganese 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 Manganese with other atoms in the Mn 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:Mn1003

b:15.0
occ:1.00
O4P B:PGA1006 1.8 20.0 1.0
OD1 B:ASP266 1.9 10.3 1.0
OE1 B:GLU242 2.0 16.6 1.0
O1P B:PGA1006 2.5 20.0 1.0
P B:PGA1006 2.7 20.0 1.0
CG B:ASP266 2.7 10.3 1.0
CD B:GLU242 3.1 16.6 1.0
OD2 B:ASP266 3.5 10.3 1.0
OE2 B:GLU242 3.5 16.6 1.0
CB B:ASP266 3.6 10.3 1.0
C2 B:PGA1006 3.6 20.0 1.0
CZ B:PHE214 3.7 7.9 1.0
O3P B:PGA1006 3.7 20.0 1.0
O1 B:PGA1006 3.8 20.0 1.0
O2P B:PGA1006 3.9 20.0 1.0
CE1 B:PHE214 4.0 7.9 1.0
N B:ASP266 4.0 2.0 1.0
C1 B:PGA1006 4.1 20.0 1.0
CG B:GLU242 4.4 16.6 1.0
CE2 B:PHE214 4.4 7.9 1.0
CA B:ASP266 4.4 2.0 1.0
CB B:GLU242 4.5 16.6 1.0
OG B:SER213 4.7 14.2 1.0
CB B:ALA263 4.8 20.3 1.0
CD1 B:PHE214 4.9 7.9 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: Tue Dec 15 03:46:02 2020

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