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Magnesium in PDB 1os1: Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate.

Enzymatic activity of Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate.

All present enzymatic activity of Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate.:
4.1.1.49;

Protein crystallography data

The structure of Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate., PDB code: 1os1 was solved by A.Sudom, R.Walters, L.Pastushok, D.Goldie, L.Prasad, L.T.Delbaere, H.Goldie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 126.200, 95.200, 46.800, 90.00, 95.20, 90.00
R / Rfree (%) 20 / 25

Other elements in 1os1:

The structure of Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate. also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate. (pdb code 1os1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate., PDB code: 1os1:

Magnesium binding site 1 out of 1 in 1os1

Go back to Magnesium Binding Sites List in 1os1
Magnesium binding site 1 out of 1 in the Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Phosphoenolpyruvate Carboxykinase Complexed with Atp,Mg, Ca and Pyruvate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg998

b:55.5
occ:1.00
 OG1 A:THR255 2.0 20.3 1.0
O A:HOH716 2.0 45.5 1.0
O A:HOH738 2.0 30.7 1.0
O A:HOH674 2.1 26.0 1.0
O3G A:ATP541 2.3 48.1 1.0
O2B A:ATP541 2.7 43.4 1.0
OD1 A:ASP268 3.1 21.1 1.0
O A:TYR286 3.2 21.5 1.0
CB A:THR255 3.3 18.8 1.0
PG A:ATP541 3.7 50.4 1.0
PB A:ATP541 3.9 44.3 1.0
O2A A:ATP541 3.9 42.2 1.0
O A:ASP268 4.1 17.8 1.0
CG2 A:THR255 4.1 22.4 1.0
CG A:ASP268 4.1 17.0 1.0
O3B A:ATP541 4.1 48.3 1.0
C A:TYR286 4.2 19.5 1.0
CA A:THR255 4.3 18.1 1.0
OD1 A:ASP269 4.3 16.6 1.0
N A:THR255 4.4 17.5 1.0
NH1 A:ARG333 4.5 20.0 1.0
O A:HOH719 4.5 52.2 1.0
O1G A:ATP541 4.6 47.6 1.0
O2G A:ATP541 4.7 46.8 1.0
O A:HOH603 4.7 25.3 1.0
PA A:ATP541 4.7 38.8 1.0
O3A A:ATP541 4.7 41.5 1.0
CB A:ASP268 4.7 17.0 1.0
CG A:ASP269 4.8 14.5 1.0
CA A:ALA287 4.8 16.0 1.0
CB A:ASP269 4.9 13.8 1.0
OD2 A:ASP268 4.9 20.7 1.0
C A:ASP268 4.9 15.1 1.0
N A:ALA287 4.9 18.0 1.0

Reference:

A.Sudom, R.Walters, L.Pastushok, D.Goldie, L.Prasad, L.T.Delbaere, H.Goldie. Mechanisms of Activation of Phosphoenolpyruvate Carboxykinase From Escherichia Coli By CA2+ and of Desensitization By Trypsin. J.Bacteriol. V. 185 4233 2003.
ISSN: ISSN 0021-9193
PubMed: 12837799
DOI: 10.1128/JB.185.14.4233-4242.2003
Page generated: Tue Aug 13 10:42:05 2024

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