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Magnesium in PDB 1zeb: X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp

Enzymatic activity of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp

All present enzymatic activity of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp:
3.1.3.1;

Protein crystallography data

The structure of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp, PDB code: 1zeb was solved by P.Llinas, E.A.Stura, A.Menez, Z.Kiss, T.Stigbrand, J.L.Millan, M.H.Le Du, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.96 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.022, 113.894, 106.594, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 19.7

Other elements in 1zeb:

The structure of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp (pdb code 1zeb). 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 X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp, PDB code: 1zeb:

Magnesium binding site 1 out of 1 in 1zeb

Go back to Magnesium Binding Sites List in 1zeb
Magnesium binding site 1 out of 1 in the X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Alkaline Phosphatase From Human Placenta in Complex with 5'-Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg903

b:10.8
occ:1.00
 O A:HOH927 2.0 12.5 1.0
O A:HOH910 2.1 12.7 1.0
OE2 A:GLU311 2.1 11.8 1.0
OD2 A:ASP42 2.1 10.9 1.0
O A:HOH937 2.2 10.9 1.0
OG A:SER155 2.2 12.2 1.0
CG A:ASP42 3.1 12.0 1.0
CD A:GLU311 3.1 12.7 1.0
CB A:SER155 3.2 13.2 1.0
OE1 A:GLU311 3.5 12.8 1.0
CB A:ASP42 3.7 12.7 1.0
CD2 A:HIS153 4.1 13.9 1.0
O A:HOH965 4.1 14.2 1.0
N A:SER155 4.1 13.3 1.0
OD1 A:ASP42 4.1 14.2 1.0
OG A:SEP92 4.2 15.3 1.0
CA A:SER155 4.2 13.4 1.0
O2P A:SEP92 4.3 12.8 1.0
O A:GLY313 4.4 12.3 1.0
CG A:GLU311 4.4 11.6 1.0
CB A:SEP92 4.4 14.1 1.0
CA A:GLY313 4.5 12.9 1.0
O A:HOH942 4.5 13.7 1.0
CG2 A:THR149 4.7 12.3 1.0
ZN A:ZN902 4.7 14.9 1.0
OG1 A:THR149 4.8 13.0 1.0
OD2 A:ASP357 4.8 12.7 1.0
CD A:PRO156 4.8 14.0 1.0
P A:SEP92 4.9 15.3 1.0
NE2 A:HIS153 4.9 15.7 1.0
C A:GLY313 5.0 12.8 1.0
CG A:HIS153 5.0 14.2 1.0

Reference:

P.Llinas, E.A.Stura, A.Menez, Z.Kiss, T.Stigbrand, J.L.Millan, M.H.Le Du. Structural Studies of Human Placental Alkaline Phosphatase in Complex with Functional Ligands. J.Mol.Biol. V. 350 441 2005.
ISSN: ISSN 0022-2836
PubMed: 15946677
DOI: 10.1016/J.JMB.2005.04.068
Page generated: Tue Aug 13 20:09:06 2024

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