Magnesium in PDB 1xon: Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast

All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast:
3.1.4.17;

The structure of Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast, PDB code: 1xon was solved by G.L.Card, B.P.England, Y.Suzuki, D.Fong, B.Powell, B.Lee, C.Luu, M.Tabrizizad, S.Gillette, P.N.Ibrahim, D.R.Artis, G.Bollag, M.V.Milburn, S.-H.Kim, J.Schlessinger, K.Y.J.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	81.65 / 1.72
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.196, 78.877, 164.312, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 19.9

The structure of Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Zinc	(Zn)	2 atoms

The binding sites of Magnesium atom in the Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast (pdb code 1xon). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast, PDB code: 1xon:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:8.7 occ:1.00 O A:HOH1007 2.0 12.9 1.0 OD1 A:ASP201 2.1 7.0 1.0 O A:HOH1003 2.1 10.7 1.0 O A:HOH1006 2.2 10.5 1.0 O A:HOH1004 2.2 11.2 1.0 O A:HOH1005 2.2 14.6 1.0 CG A:ASP201 3.1 7.4 1.0 OD2 A:ASP201 3.4 7.7 1.0 ZN A:ZN1001 3.8 15.3 1.0 OE2 A:GLU230 4.0 8.7 1.0 O A:HOH1008 4.1 10.2 1.0 NE2 A:HIS233 4.1 6.8 1.0 N22 A:PIL501 4.1 16.9 1.0 O A:HIS200 4.1 6.7 1.0 CD2 A:HIS200 4.2 6.8 1.0 O A:HOH1019 4.2 17.1 1.0 OG1 A:THR271 4.3 7.6 1.0 CD2 A:HIS233 4.3 7.1 1.0 OD2 A:ASP318 4.4 9.4 1.0 CB A:ASP201 4.5 7.5 1.0 C21 A:PIL501 4.5 16.2 1.0 CD2 A:HIS204 4.6 7.4 1.0 C23 A:PIL501 4.6 16.8 1.0 O A:HOH1073 4.6 23.4 1.0 NE2 A:HIS200 4.7 5.4 1.0 CD2 A:HIS160 4.7 7.0 1.0 NE2 A:HIS204 4.8 7.4 1.0 NE2 A:HIS160 4.8 9.1 1.0 CG A:GLU230 4.8 7.7 1.0 CA A:ASP201 4.8 7.2 1.0 CB A:THR271 4.8 8.1 1.0 CD A:GLU230 4.9 8.2 1.0 O A:THR271 4.9 8.9 1.0 C A:HIS200 4.9 6.8 1.0

Magnesium binding site 2 out of 2 in the Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catalytic Domain of Human Phosphodiesterase 4D in Complex with Piclamilast within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:9.6 occ:1.00 O B:HOH2004 2.1 12.5 1.0 O B:HOH2005 2.1 13.7 1.0 O B:HOH2003 2.1 13.1 1.0 O B:HOH2006 2.1 14.2 1.0 O B:HOH2007 2.1 14.4 1.0 OD1 B:ASP201 2.1 8.1 1.0 CG B:ASP201 3.2 7.3 1.0 OD2 B:ASP201 3.5 8.0 1.0 ZN B:ZN1001 3.8 16.4 1.0 OE2 B:GLU230 4.0 10.9 1.0 N22 B:PIL502 4.1 16.9 1.0 CD2 B:HIS200 4.1 8.8 1.0 O B:HOH2014 4.1 13.4 1.0 O B:HIS200 4.1 7.5 1.0 NE2 B:HIS233 4.1 7.2 1.0 O B:HOH2008 4.2 11.2 1.0 OG1 B:THR271 4.3 10.5 1.0 CD2 B:HIS233 4.3 6.4 1.0 C21 B:PIL502 4.5 16.7 1.0 OD2 B:ASP318 4.5 8.8 1.0 CB B:ASP201 4.5 7.0 1.0 C23 B:PIL502 4.6 16.7 1.0 CD2 B:HIS204 4.6 9.4 1.0 NE2 B:HIS200 4.6 6.7 1.0 O B:HOH2062 4.6 24.1 1.0 NE2 B:HIS160 4.7 8.8 1.0 CD2 B:HIS160 4.8 7.1 1.0 CB B:THR271 4.8 9.4 1.0 CA B:ASP201 4.8 7.3 1.0 NE2 B:HIS204 4.8 7.4 1.0 CD B:GLU230 4.8 9.6 1.0 CG B:GLU230 4.8 7.6 1.0 O B:THR271 5.0 10.3 1.0 C B:HIS200 5.0 7.5 1.0

G.L.Card, B.P.England, Y.Suzuki, D.Fong, B.Powell, B.Lee, C.Luu, M.Tabrizizad, S.Gillette, P.N.Ibrahim, D.R.Artis, G.Bollag, M.V.Milburn, S.-H.Kim, J.Schlessinger, K.Y.J.Zhang. Structural Basis For the Activity of Drugs That Inhibit Phosphodiesterases. Structure V. 12 2233 2004.
ISSN: ISSN 0969-2126
PubMed: 15576036
DOI: 10.1016/J.STR.2004.10.004