Zinc in PDB 1zef: 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;

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

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
Calcium	(Ca)	1 atom

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Alkaline Phosphatase From Human Placenta in Complex with Its Uncompetitive Inhibitor L-Phe, PDB code: 1zef:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 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 Zinc with other atoms in the Zn 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:Zn901 b:14.9 occ:1.00 NE2 A:HIS432 2.0 11.4 1.0 OD1 A:ASP316 2.0 14.4 1.0 NE2 A:HIS320 2.1 14.4 1.0 O3P A:SEP92 2.2 14.5 1.0 N A:PHE802 2.2 39.4 1.0 OD2 A:ASP316 2.4 13.7 1.0 CA A:PHE802 2.5 41.9 1.0 CG A:ASP316 2.6 14.4 1.0 CE1 A:HIS432 3.0 13.8 1.0 CD2 A:HIS432 3.0 14.3 1.0 CE1 A:HIS320 3.0 19.3 1.0 CD2 A:HIS320 3.1 18.3 1.0 P A:SEP92 3.2 15.8 1.0 CB A:PHE802 3.4 42.4 1.0 O1P A:SEP92 3.6 15.7 1.0 C A:PHE802 3.7 43.2 1.0 O2P A:SEP92 3.9 14.3 1.0 O A:HOH905 3.9 13.3 1.0 O A:PHE802 3.9 43.7 1.0 ZN A:ZN902 4.0 15.0 1.0 CB A:ASP316 4.1 12.5 1.0 NE2 A:HIS358 4.1 16.3 1.0 ND1 A:HIS432 4.1 12.3 1.0 CG A:HIS432 4.1 14.3 1.0 ND1 A:HIS320 4.2 16.2 1.0 CG A:HIS320 4.2 15.1 1.0 CG A:PHE802 4.2 44.2 1.0 NE2 A:HIS360 4.3 19.1 1.0 CE1 A:HIS358 4.4 12.5 1.0 CD2 A:PHE802 4.4 47.3 1.0 OD1 A:ASP42 4.5 12.7 1.0 OG A:SEP92 4.5 14.4 1.0 CE1 A:HIS360 4.6 13.2 1.0 OXT A:PHE802 4.6 44.1 1.0 O A:ASP316 4.9 11.5 1.0 CA A:ASP316 5.0 12.7 1.0 C A:ASP316 5.0 12.2 1.0

Zinc binding site 2 out of 2 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 Zinc with other atoms in the Zn binding site number 2 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:Zn902 b:15.0 occ:1.00 OD1 A:ASP42 1.9 12.7 1.0 CE1 A:HIS358 2.0 12.5 1.0 OD2 A:ASP357 2.1 13.6 1.0 OG A:SEP92 2.1 14.4 1.0 O3P A:SEP92 2.2 14.5 1.0 CG A:ASP42 2.7 10.6 1.0 OD2 A:ASP42 2.9 13.1 1.0 P A:SEP92 2.9 15.8 1.0 CG A:ASP357 2.9 15.2 1.0 ND1 A:HIS358 3.0 17.5 1.0 NE2 A:HIS358 3.0 16.3 1.0 OD1 A:ASP357 3.0 12.3 1.0 CB A:SEP92 3.4 13.6 1.0 OD2 A:ASP316 3.7 13.7 1.0 O1P A:SEP92 3.8 15.7 1.0 CA A:SEP92 3.9 14.0 1.0 O2P A:SEP92 3.9 14.3 1.0 CG A:ASP316 3.9 14.4 1.0 CE1 A:HIS432 4.0 13.8 1.0 ZN A:ZN901 4.0 14.9 1.0 CB A:ASP42 4.1 13.2 1.0 CD2 A:HIS358 4.2 10.7 1.0 CG A:HIS358 4.2 13.0 1.0 NE2 A:HIS432 4.2 11.4 1.0 N A:SEP92 4.2 15.1 1.0 OD1 A:ASP316 4.2 14.4 1.0 N A:GLY43 4.2 13.1 1.0 CB A:ASP357 4.3 12.7 1.0 O A:HOH945 4.4 12.8 1.0 CA A:ASP42 4.4 12.9 1.0 C A:ASP42 4.5 12.5 1.0 CB A:ASP316 4.5 12.5 1.0 O A:HOH905 4.6 13.3 1.0 MG A:MG903 4.7 13.0 1.0 N A:PHE802 4.7 39.4 1.0 O A:HOH957 4.7 13.5 1.0 ND1 A:HIS432 4.8 12.3 1.0 C A:ASP91 4.9 14.1 1.0 CA A:GLY43 4.9 12.1 1.0

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