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Manganese 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:

Magnesium (Mg) 1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of E. Coli Phosphoenolpyruvate Carboxykinase Mutant LYS213SER Complexed with Atp-MG2+-MN2+, PDB code: 2py7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2py7

Go back to Manganese Binding Sites List in 2py7
Manganese binding site 1 out of 2 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 Manganese with other atoms in the Mn 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:Mn999

b:9.7
occ:1.00
OD2 X:ASP269 2.0 8.4 1.0
O1G X:ATP541 2.2 13.6 1.0
NE2 X:HIS232 2.2 3.5 1.0
O X:HOH1373 2.2 17.6 1.0
CG X:ASP269 2.8 8.8 1.0
OD1 X:ASP269 2.8 9.7 1.0
CD2 X:HIS232 3.1 5.3 1.0
CE1 X:HIS232 3.2 4.2 1.0
PG X:ATP541 3.3 14.1 1.0
O X:HOH1375 3.4 21.0 1.0
O3G X:ATP541 3.7 14.3 1.0
O2G X:ATP541 4.0 12.6 1.0
NZ X:LYS254 4.0 8.0 1.0
CE X:LYS254 4.1 8.1 1.0
O X:HOH1022 4.1 9.4 1.0
CB X:ASP269 4.2 7.6 1.0
CG X:HIS232 4.3 5.1 1.0
ND1 X:HIS232 4.3 4.2 1.0
O X:HOH1386 4.3 22.6 1.0
O X:HOH1481 4.5 33.3 1.0
O3B X:ATP541 4.6 15.8 1.0
O X:ASP269 4.8 7.6 1.0
NZ X:LYS212 4.9 9.9 1.0
CE2 X:PHE413 4.9 5.2 1.0
MG X:MG998 4.9 2.3 1.0
CA X:ASP269 5.0 7.6 1.0

Manganese binding site 2 out of 2 in 2py7

Go back to Manganese Binding Sites List in 2py7
Manganese binding site 2 out of 2 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 Manganese with other atoms in the Mn binding site number 2 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:Mn1001

b:24.7
occ:1.00
NE2 X:HIS21 2.1 26.4 1.0
OD2 X:ASP19 2.1 24.0 1.0
OD1 X:ASP19 2.3 24.2 1.0
O X:HOH1488 2.4 28.0 1.0
CG X:ASP19 2.5 22.8 1.0
CE1 X:HIS21 2.9 26.4 1.0
CD2 X:HIS21 3.2 25.5 1.0
O X:HOH1296 4.0 33.1 1.0
CB X:ASP19 4.0 20.9 1.0
ND1 X:HIS21 4.0 25.9 1.0
CG X:HIS21 4.2 24.5 1.0
O X:ASP19 4.5 20.9 1.0
CA X:ASP19 4.8 20.6 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: Sat Oct 5 14:57:32 2024

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