Magnesium in PDB 1w6r: Complex of Tcache with Galanthamine Derivative

All present enzymatic activity of Complex of Tcache with Galanthamine Derivative:
3.1.1.7;

The structure of Complex of Tcache with Galanthamine Derivative, PDB code: 1w6r was solved by H.M.Greenblatt, C.Guillou, D.Guenard, B.Badet, C.Thal, I.Silman, J.L.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.32 / 2.05
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	111.751, 111.751, 137.173, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 23.2

The binding sites of Magnesium atom in the Complex of Tcache with Galanthamine Derivative (pdb code 1w6r). 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 Complex of Tcache with Galanthamine Derivative, PDB code: 1w6r:

Magnesium binding site 1 out of 1 in the Complex of Tcache with Galanthamine Derivative


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex of Tcache with Galanthamine Derivative within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1537 b:48.3 occ:1.00 O A:HOH2164 2.0 43.7 1.0 OD1 A:ASP326 2.1 34.9 1.0 O A:HOH2167 2.1 47.1 1.0 OD2 A:ASP392 2.1 44.8 1.0 O A:HOH2190 2.2 39.2 1.0 O A:HOH2192 2.2 47.5 1.0 CG A:ASP326 3.2 35.2 1.0 CG A:ASP392 3.3 40.0 1.0 CB A:ASP326 3.8 33.3 1.0 CB A:ASP392 4.0 39.3 1.0 OD1 A:ASP393 4.0 38.5 1.0 CA A:ASP326 4.1 32.6 1.0 O A:LYS325 4.2 30.5 1.0 O A:HOH2211 4.2 50.5 1.0 OD2 A:ASP326 4.3 34.5 1.0 OD1 A:ASP392 4.3 39.6 1.0 O A:ASP389 4.5 36.3 1.0 NZ A:LYS325 4.5 47.4 1.0 CG A:ASP393 4.6 39.6 1.0 O A:HOH2083 4.6 51.9 1.0 OD2 A:ASP393 4.7 39.4 1.0 C A:LYS325 4.7 33.5 1.0 N A:ASP326 4.8 33.0 1.0 O A:HOH2195 4.9 57.4 1.0 CE A:LYS325 4.9 45.0 1.0 OD1 A:ASP389 5.0 38.4 1.0 CB A:ASP389 5.0 38.1 1.0 N A:ASP393 5.0 36.8 1.0

H.M.Greenblatt, C.Guillou, D.Guenard, A.Argaman, S.Botti, B.Badet, C.Thal, I.Silman, J.L.Sussman. The Complex of A Bivalent Derivative of Galanthamine with Torpedo Acetylcholinesterase Displays Drastic Deformation of the Active-Site Gorge: Implications For Structure-Based Drug Design. J.Am.Chem.Soc. V. 126 15405 2004.
ISSN: ISSN 0002-7863
PubMed: 15563167
DOI: 10.1021/JA0466154