Magnesium in PDB 7b56: Crystal Structure of Camkii-Actinin Complex Bound to Amppnp

All present enzymatic activity of Crystal Structure of Camkii-Actinin Complex Bound to Amppnp:
2.7.11.17;

The structure of Crystal Structure of Camkii-Actinin Complex Bound to Amppnp, PDB code: 7b56 was solved by J.Zhu, M.Gold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.77 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.426, 72.51, 92.001, 90, 90, 90
R / Rfree (%)	19 / 21.5

The binding sites of Magnesium atom in the Crystal Structure of Camkii-Actinin Complex Bound to Amppnp (pdb code 7b56). 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 Crystal Structure of Camkii-Actinin Complex Bound to Amppnp, PDB code: 7b56:

Magnesium binding site 1 out of 1 in the Crystal Structure of Camkii-Actinin Complex Bound to Amppnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Camkii-Actinin Complex Bound to Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:24.1 occ:1.00 O2B B:ANP401 2.0 24.3 1.0 O1G B:ANP401 2.0 26.7 1.0 O B:HOH624 2.0 30.8 1.0 O B:HOH706 2.0 25.7 1.0 OD1 B:ASP156 2.2 21.4 1.0 OD2 B:ASP156 2.3 25.3 1.0 CG B:ASP156 2.6 24.1 1.0 PG B:ANP401 3.2 26.6 1.0 PB B:ANP401 3.2 24.4 1.0 N3B B:ANP401 3.5 23.8 1.0 O B:HOH704 3.8 28.2 1.0 O2G B:ANP401 3.8 26.9 1.0 O B:HOH667 3.9 33.2 1.0 CA B:GLY158 4.0 21.4 1.0 O1B B:ANP401 4.0 24.0 1.0 CB B:ASP156 4.1 20.2 1.0 O B:HOH623 4.1 31.2 1.0 O B:HOH795 4.2 38.9 1.0 N B:GLY158 4.3 20.2 1.0 O B:HOH517 4.3 29.6 1.0 NZ B:LYS42 4.4 22.6 1.0 O3A B:ANP401 4.4 21.7 1.0 O3G B:ANP401 4.5 29.0 1.0 O B:HOH555 4.7 31.9 1.0 O2A B:ANP401 4.7 22.3 1.0 N A:SER822 4.7 26.3 1.0 CA B:ASP156 4.8 19.1 1.0 C B:GLY158 4.8 21.4 1.0 PA B:ANP401 4.9 21.6 1.0

J.Zhu, M.Gold. Crystal Structure of Camkii-Actinin Complex Bound to Mes To Be Published.