Magnesium in PDB 1xlx: Catalytic Domain of Human Phosphodiesterase 4B in Complex with Cilomilast

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

The structure of Catalytic Domain of Human Phosphodiesterase 4B in Complex with Cilomilast, PDB code: 1xlx 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)	70.71 / 2.19
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.274, 94.259, 106.078, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 28.2

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

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Catalytic Domain of Human Phosphodiesterase 4B in Complex with Cilomilast (pdb code 1xlx). 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 4B in Complex with Cilomilast, PDB code: 1xlx:
Jump to Magnesium binding site number: 1; 2;

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


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 4B in Complex with Cilomilast within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:29.4 occ:1.00 O A:HOH1006 1.9 36.2 1.0 O A:HOH1003 2.0 44.0 1.0 O A:HOH1004 2.2 33.2 1.0 O A:HOH1007 2.2 34.6 1.0 OD1 A:ASP275 2.2 22.0 1.0 O A:HOH1005 2.3 31.2 1.0 CG A:ASP275 3.2 22.6 1.0 OD2 A:ASP275 3.5 25.4 1.0 O25 A:CIO101 3.6 51.5 1.0 ZN A:ZN1001 3.9 37.2 1.0 O A:HOH61 4.0 47.4 1.0 OG1 A:THR345 4.1 24.0 1.0 O A:HOH1008 4.1 22.5 1.0 C23 A:CIO101 4.1 52.4 1.0 OE2 A:GLU304 4.2 25.3 1.0 NE2 A:HIS307 4.2 18.7 1.0 CD2 A:HIS307 4.4 16.8 1.0 O A:HIS274 4.4 20.9 1.0 CD2 A:HIS274 4.5 13.7 1.0 O A:THR345 4.5 24.5 1.0 CB A:ASP275 4.6 21.8 1.0 O24 A:CIO101 4.6 49.7 1.0 CB A:THR345 4.6 22.9 1.0 CD2 A:HIS278 4.6 18.3 1.0 OD1 A:ASP392 4.8 27.8 1.0 NE2 A:HIS274 4.8 17.6 1.0 CG A:GLU304 4.8 20.0 1.0 CD A:GLU304 4.9 24.0 1.0 C4 A:CIO101 4.9 50.8 1.0 CA A:ASP275 4.9 21.0 1.0 C3 A:CIO101 4.9 50.2 1.0 CD2 A:HIS234 5.0 21.8 1.0

Magnesium binding site 2 out of 2 in the Catalytic Domain of Human Phosphodiesterase 4B in Complex with Cilomilast


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 4B in Complex with Cilomilast within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:30.2 occ:1.00 O B:HOH2006 2.0 34.9 1.0 OD1 B:ASP275 2.1 25.1 1.0 O B:HOH2004 2.1 33.4 1.0 O B:HOH2007 2.1 30.4 1.0 O B:HOH2005 2.2 36.1 1.0 O B:HOH2003 2.2 40.2 1.0 CG B:ASP275 3.1 24.1 1.0 OD2 B:ASP275 3.4 27.1 1.0 ZN B:ZN1001 3.7 39.8 1.0 OG1 B:THR345 3.9 20.7 1.0 O B:HIS274 4.0 26.4 1.0 CD2 B:HIS274 4.0 14.9 1.0 O B:HOH2008 4.1 41.3 1.0 O25 B:CIO102 4.1 62.5 1.0 OE2 B:GLU304 4.1 23.1 1.0 NE2 B:HIS307 4.1 23.0 1.0 C23 B:CIO102 4.4 58.7 1.0 CD2 B:HIS307 4.4 18.1 1.0 OD1 B:ASP392 4.4 28.0 1.0 O B:HOH62 4.4 44.8 1.0 CB B:ASP275 4.5 22.4 1.0 NE2 B:HIS274 4.5 6.3 1.0 CD2 B:HIS278 4.6 19.5 1.0 O B:THR345 4.6 21.4 1.0 O24 B:CIO102 4.7 56.6 1.0 CA B:ASP275 4.7 22.2 1.0 CB B:THR345 4.8 20.7 1.0 NE2 B:HIS278 4.8 24.1 1.0 NE2 B:HIS234 4.9 22.4 1.0 CD2 B:HIS234 4.9 18.4 1.0 C B:HIS274 4.9 23.4 1.0 C4 B:CIO102 5.0 54.1 1.0 CD B:GLU304 5.0 23.0 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