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Calcium in PDB 1zef: Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe

Enzymatic activity of Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe

All present enzymatic activity of Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe:
3.1.3.1;

Protein crystallography data

The structure of Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe, PDB code: 1zef 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) 15.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 87.791, 114.944, 106.341, 90.00, 90.00, 90.00
R / Rfree (%) 12.6 / 17.3

Other elements in 1zef:

The structure of Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe (pdb code 1zef). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe, PDB code: 1zef:

Calcium binding site 1 out of 1 in 1zef

Go back to Calcium Binding Sites List in 1zef
Calcium binding site 1 out of 1 in the Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca904

b:16.3
occ:1.00
 OE2 A:GLU270 2.1 23.4 1.0
OE1 A:GLU216 2.2 20.6 1.0
O A:PHE269 2.2 17.5 1.0
OD2 A:ASP285 2.2 23.0 1.0
O A:HOH1158 2.3 24.4 1.0
OE2 A:GLU216 2.4 23.0 1.0
OD1 A:ASP285 2.5 25.8 1.0
CD A:GLU216 2.6 25.3 1.0
CG A:ASP285 2.7 23.6 1.0
CD A:GLU270 3.2 21.6 1.0
C A:PHE269 3.4 16.2 1.0
CG A:GLU270 3.9 16.6 1.0
OE1 A:GLU270 4.1 19.0 1.0
CG A:GLU216 4.2 25.4 1.0
CB A:ASP285 4.2 20.4 1.0
CA A:PHE269 4.3 16.4 1.0
N A:GLU270 4.4 15.9 1.0
O A:LEU284 4.4 20.4 1.0
O A:HOH934 4.4 24.0 1.0
CA A:GLU270 4.4 16.2 1.0
CB A:PHE269 4.4 16.1 1.0
CB A:LEU284 4.5 24.0 1.0
NH2 A:ARG204 4.5 21.0 1.0
O A:TRP248 4.5 20.1 1.0
O A:HOH977 4.5 21.3 1.0
O A:HOH1356 4.6 50.4 1.0
OH A:TYR217 4.6 23.2 1.0
NH1 A:ARG204 4.6 20.3 1.0
C A:LEU284 4.6 21.6 1.0
O A:HOH1413 4.7 54.4 1.0
CB A:GLU270 4.7 16.4 1.0
CA A:ASP285 4.8 20.3 1.0
CB A:GLU216 4.9 25.3 1.0
N A:ASP285 4.9 21.0 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: Fri Jul 12 08:22:57 2024

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