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Magnesium in PDB 1zed: Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate

Enzymatic activity of Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate

All present enzymatic activity of Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate:
3.1.3.1;

Protein crystallography data

The structure of Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate, PDB code: 1zed 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) 24.92 / 1.57
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 88.346, 114.573, 106.568, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 18.8

Other elements in 1zed:

The structure of Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate 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 Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate (pdb code 1zed). 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 Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate, PDB code: 1zed:

Magnesium binding site 1 out of 1 in 1zed

Go back to Magnesium Binding Sites List in 1zed
Magnesium binding site 1 out of 1 in the Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alkaline Phosphatase From Human Placenta in Complex with P- Nitrophenyl-Phosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg905

b:3.4
occ:1.00
 OD2 A:ASP42 2.0 12.7 1.0
OE2 A:GLU311 2.0 13.7 1.0
O A:HOH969 2.1 13.8 1.0
O A:HOH949 2.1 13.0 1.0
O A:HOH1038 2.2 14.6 1.0
OG A:SER155 2.2 13.2 1.0
CG A:ASP42 3.0 12.5 1.0
CD A:GLU311 3.0 12.2 1.0
CB A:SER155 3.2 12.9 1.0
OE1 A:GLU311 3.5 12.9 1.0
CB A:ASP42 3.5 12.5 1.0
OD1 A:ASP42 4.0 11.0 1.0
O A:HOH1667 4.0 15.2 1.0
CD2 A:HIS153 4.0 13.8 1.0
N A:SER155 4.1 13.2 1.0
CA A:SER155 4.2 12.9 1.0
OG A:SER92 4.3 11.0 1.0
CG A:GLU311 4.3 12.4 1.0
O1 A:PO3907 4.4 14.8 1.0
O A:GLY313 4.4 13.2 1.0
O A:HOH993 4.4 12.6 1.0
CA A:GLY313 4.5 12.4 1.0
CB A:SER92 4.5 13.0 1.0
ZN A:ZN904 4.7 12.5 1.0
CG2 A:THR149 4.7 12.3 1.0
OD2 A:ASP357 4.8 9.3 1.0
OG1 A:THR149 4.8 13.9 1.0
CD A:PRO156 4.8 12.6 1.0
NE2 A:HIS153 4.8 17.4 1.0
CA A:ASP42 4.9 12.2 1.0
C A:GLY313 4.9 12.4 1.0
P A:PO3907 5.0 15.1 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 20:09:19 2024

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