Magnesium in PDB 1taz: Catalytic Domain of Human Phosphodiesterase 1B

All present enzymatic activity of Catalytic Domain of Human Phosphodiesterase 1B:
3.1.4.17;

The structure of Catalytic Domain of Human Phosphodiesterase 1B, PDB code: 1taz was solved by K.Y.J.Zhang, G.L.Card, Y.Suzuki, D.R.Artis, D.Fong, S.Gillette, D.Hsieh, J.Neiman, B.L.West, C.Zhang, M.V.Milburn, S.-H.Kim, J.Schlessinger, G.Bollag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.55 / 1.77
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	87.232, 87.232, 134.151, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 19.3

The structure of Catalytic Domain of Human Phosphodiesterase 1B also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Catalytic Domain of Human Phosphodiesterase 1B (pdb code 1taz). 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 Catalytic Domain of Human Phosphodiesterase 1B, PDB code: 1taz:

Magnesium binding site 1 out of 1 in the Catalytic Domain of Human Phosphodiesterase 1B


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 1B within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:17.6 occ:1.00 O A:HOH1004 2.1 16.0 1.0 OD1 A:ASP264 2.1 15.2 1.0 O A:HOH1007 2.1 16.1 1.0 O A:HOH1003 2.1 15.1 1.0 O A:HOH1005 2.2 17.6 1.0 O A:HOH1006 2.2 17.9 1.0 CG A:ASP264 3.1 17.1 1.0 OD2 A:ASP264 3.4 17.1 1.0 ZN A:ZN1001 3.8 22.1 1.0 OE2 A:GLU293 4.1 19.8 1.0 O A:HIS263 4.2 16.8 1.0 CD2 A:HIS263 4.2 16.5 1.0 NE2 A:HIS296 4.2 15.0 1.0 O A:HOH1008 4.2 21.7 1.0 OG1 A:THR334 4.2 18.7 1.0 O A:HOH1068 4.3 38.0 1.0 O A:HOH1010 4.3 25.6 1.0 CD2 A:HIS267 4.3 17.3 1.0 CB A:ASP264 4.5 16.2 1.0 CD2 A:HIS296 4.5 15.6 1.0 NE2 A:HIS267 4.5 16.4 1.0 OD2 A:ASP370 4.5 22.4 1.0 NE2 A:HIS263 4.6 16.4 1.0 NE2 A:HIS223 4.7 19.9 1.0 CD2 A:HIS223 4.7 19.0 1.0 CB A:THR334 4.7 18.8 1.0 O A:THR334 4.8 19.7 1.0 CA A:ASP264 4.8 16.1 1.0 CG A:GLU293 4.8 17.5 1.0 O A:HOH1086 4.8 38.9 1.0 CD A:GLU293 4.9 19.8 1.0 C A:HIS263 5.0 16.3 1.0

K.Y.J.Zhang, G.L.Card, Y.Suzuki, D.R.Artis, D.Fong, S.Gillette, D.Hsieh, J.Neiman, B.L.West, C.Zhang, M.V.Milburn, S.-H.Kim, J.Schlessinger, G.Bollag. A Glutamine Switch Mechanism For Nucleotide Selectivity By Phosphodiesterases Mol.Cell V. 15 279 2004.
ISSN: ISSN 1097-2765
PubMed: 15260978
DOI: 10.1016/J.MOLCEL.2004.07.005