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Magnesium in PDB 2py7: Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+

Enzymatic activity of Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+

All present enzymatic activity of Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+:
4.1.1.49;

Protein crystallography data

The structure of Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+, PDB code: 2py7 was solved by L.T.J.Delbaere, J.J.H.Cotelesage, H.Goldie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.48 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 124.999, 95.663, 46.319, 90.00, 96.12, 90.00
R / Rfree (%) 15.5 / 21.8

Other elements in 2py7:

The structure of Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+ also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+ (pdb code 2py7). 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 Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+, PDB code: 2py7:

Magnesium binding site 1 out of 1 in 2py7

Go back to Magnesium Binding Sites List in 2py7
Magnesium binding site 1 out of 1 in the Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Mg998

b:2.3
occ:1.00
O2B X:ATP541 1.8 16.6 1.0
O3G X:ATP541 1.9 14.3 1.0
OG1 X:THR255 2.1 9.2 1.0
O X:HOH1022 2.2 9.4 1.0
O X:HOH1040 2.2 8.2 1.0
O X:HOH1012 2.2 4.8 1.0
PB X:ATP541 3.1 15.3 1.0
PG X:ATP541 3.1 14.1 1.0
CB X:THR255 3.2 10.0 1.0
O3B X:ATP541 3.4 15.8 1.0
O2A X:ATP541 3.8 16.6 1.0
O1G X:ATP541 3.9 13.6 1.0
O3A X:ATP541 4.0 15.6 1.0
O X:HOH1375 4.0 21.0 1.0
OD2 X:ASP268 4.0 13.9 1.0
N X:THR255 4.0 10.2 1.0
O X:TYR286 4.0 8.0 1.0
CA X:THR255 4.2 10.3 1.0
OD1 X:ASP268 4.2 13.6 1.0
OD2 X:ASP269 4.2 8.4 1.0
NH1 X:ARG333 4.2 5.0 1.0
PA X:ATP541 4.3 16.4 1.0
CG2 X:THR255 4.3 9.3 1.0
O2G X:ATP541 4.3 12.6 1.0
O1B X:ATP541 4.3 12.9 1.0
CG X:ASP268 4.4 9.5 1.0
O X:ASP268 4.4 7.7 1.0
O1A X:ATP541 4.6 16.9 1.0
CB X:LYS254 4.8 9.6 1.0
CG X:ASP269 4.9 8.8 1.0
CE X:LYS254 4.9 8.1 1.0
MN X:MN999 4.9 9.7 1.0
C X:LYS254 4.9 10.2 1.0
C X:TYR286 5.0 7.7 1.0

Reference:

L.T.J.Delbaere, J.J.H.Cotelesage, H.Goldie. Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER To Be Published.
Page generated: Wed Aug 14 02:20:21 2024

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