Zinc in PDB 3sni: Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors

All present enzymatic activity of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors:
3.1.4.17; 3.1.4.35;

The structure of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors, PDB code: 3sni was solved by M.S.Malamas, Y.Ni, J.Erdei, H.Stange, R.Schindler, H.-J.Lankau, C.Grunwald, K.Y.Fan, K.D.Parris, B.Langen, U.Egerland, T.Hage, K.L.Marquis, S.Grauer, J.Brennan, R.Navarra, R.Graf, B.L.Harrison, A.Robichaud, T.Kronbach, M.Pangalos, N.Hofgen, N.J.Brandon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.74 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.245, 81.337, 157.415, 90.00, 90.00, 90.00
R / Rfree (%)	24.7 / 31.9

The structure of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors (pdb code 3sni). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors, PDB code: 3sni:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn780 b:34.0 occ:1.00 OD1 A:ASP664 1.9 17.8 1.0 OD2 A:ASP554 2.0 21.9 1.0 NE2 A:HIS553 2.2 19.6 1.0 NE2 A:HIS519 2.3 22.4 1.0 O A:HOH72 2.4 13.3 1.0 O A:HOH2 2.6 34.5 1.0 CG A:ASP664 2.9 21.3 1.0 CD2 A:HIS553 2.9 21.5 1.0 CG A:ASP554 3.0 26.1 1.0 CD2 A:HIS519 3.1 20.9 1.0 OD2 A:ASP664 3.2 20.1 1.0 CE1 A:HIS519 3.4 21.4 1.0 CE1 A:HIS553 3.4 20.0 1.0 OD1 A:ASP554 3.4 24.5 1.0 MG A:MG781 3.8 14.0 1.0 CD2 A:HIS515 4.1 26.9 1.0 O A:HOH92 4.1 24.3 1.0 O A:HOH167 4.2 20.6 1.0 CG A:HIS553 4.2 23.5 1.0 CB A:ASP664 4.3 21.7 1.0 CB A:ASP554 4.3 26.4 1.0 CG A:HIS519 4.3 22.3 1.0 ND1 A:HIS553 4.3 21.7 1.0 ND1 A:HIS519 4.4 22.8 1.0 O A:HOH89 4.4 32.8 1.0 NE2 A:HIS515 4.4 27.3 1.0 CA A:ASP664 4.7 22.1 1.0 CG2 A:VAL523 4.8 22.9 1.0 O A:ASP664 4.9 22.6 1.0 O A:HOH43 5.0 14.1 1.0

Zinc binding site 2 out of 2 in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn780 b:34.2 occ:1.00 O B:HOH82 1.8 22.9 1.0 NE2 B:HIS519 2.0 22.6 1.0 NE2 B:HIS553 2.2 30.1 1.0 OD1 B:ASP664 2.2 27.6 1.0 OD2 B:ASP554 2.6 31.9 1.0 O B:HOH100 2.8 31.1 1.0 CD2 B:HIS553 3.0 29.8 1.0 CE1 B:HIS519 3.0 24.6 1.0 CD2 B:HIS519 3.0 24.3 1.0 CG B:ASP664 3.1 28.0 1.0 CG B:ASP554 3.2 32.4 1.0 CE1 B:HIS553 3.3 29.5 1.0 OD1 B:ASP554 3.4 31.3 1.0 OD2 B:ASP664 3.4 29.5 1.0 O B:HOH50 3.8 43.5 1.0 MG B:MG781 3.9 32.9 1.0 ND1 B:HIS519 4.1 24.2 1.0 CG B:HIS519 4.2 24.4 1.0 CG B:HIS553 4.2 29.9 1.0 O B:HOH44 4.3 26.2 1.0 ND1 B:HIS553 4.3 29.8 1.0 CD2 B:HIS515 4.3 27.3 1.0 CB B:ASP664 4.4 27.7 1.0 CB B:ASP554 4.4 32.7 1.0 CG2 B:VAL523 4.6 26.1 1.0 NE2 B:HIS515 4.7 27.3 1.0 CA B:ASP664 4.8 27.6 1.0 O B:ASP664 4.8 27.4 1.0 O B:HOH25 4.9 20.6 1.0

M.S.Malamas, Y.Ni, J.Erdei, H.Stange, R.Schindler, H.J.Lankau, C.Grunwald, K.Y.Fan, K.Parris, B.Langen, U.Egerland, T.Hage, K.L.Marquis, S.Grauer, J.Brennan, R.Navarra, R.Graf, B.L.Harrison, A.Robichaud, T.Kronbach, M.N.Pangalos, N.Hoefgen, N.J.Brandon. Highly Potent, Selective, and Orally Active Phosphodiesterase 10A Inhibitors. J.Med.Chem. V. 54 7621 2011.
ISSN: ISSN 0022-2623
PubMed: 21988093
DOI: 10.1021/JM2009138