Magnesium in PDB 5ium: Crystal Structure of Phosphorylated Deskc

All present enzymatic activity of Crystal Structure of Phosphorylated Deskc:
2.7.13.3;

The structure of Crystal Structure of Phosphorylated Deskc, PDB code: 5ium was solved by F.Trajtenberg, A.Buschiazzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.50 / 3.16
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.443, 94.443, 161.848, 90.00, 90.00, 120.00
R / Rfree (%)	25.7 / 29.5

The binding sites of Magnesium atom in the Crystal Structure of Phosphorylated Deskc (pdb code 5ium). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Phosphorylated Deskc, PDB code: 5ium:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Phosphorylated Deskc


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 Phosphorylated Deskc within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:0.1 occ:1.00 O1B A:ACP401 2.0 0.1 1.0 OD1 A:ASN293 2.1 0.8 1.0 O1A A:ACP401 2.1 0.1 1.0 O A:HOH501 2.2 0.6 1.0 OE2 A:GLU289 2.3 0.8 1.0 O3G A:ACP401 2.3 0.3 1.0 PB A:ACP401 3.1 0.6 1.0 CG A:ASN293 3.1 0.3 1.0 PA A:ACP401 3.2 0.4 1.0 O3A A:ACP401 3.3 0.9 1.0 PG A:ACP401 3.3 0.1 1.0 CD A:GLU289 3.3 0.5 1.0 O1G A:ACP401 3.4 0.8 1.0 ND2 A:ASN293 3.6 0.9 1.0 OE1 A:GLU289 3.7 0.6 1.0 C3B A:ACP401 3.7 0.7 1.0 NE2 A:HIS297 4.2 0.7 1.0 O5' A:ACP401 4.2 0.4 1.0 O2A A:ACP401 4.3 0.9 1.0 N A:GLY336 4.4 0.5 1.0 O2B A:ACP401 4.4 0.4 1.0 CA A:GLY336 4.5 1.0 1.0 CB A:ASN293 4.5 0.2 1.0 CG A:GLU289 4.6 0.2 1.0 O2G A:ACP401 4.7 0.3 1.0 CA A:ASN293 4.8 0.8 1.0 CD2 A:HIS297 4.9 0.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Phosphorylated Deskc


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Phosphorylated Deskc within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:0.2 occ:1.00 O1B B:ACP401 2.0 0.8 1.0 O1A B:ACP401 2.1 0.8 1.0 OD1 B:ASN293 2.1 0.9 1.0 O B:HOH502 2.1 0.5 1.0 OE2 B:GLU289 2.3 0.5 1.0 O3G B:ACP401 2.3 0.7 1.0 PB B:ACP401 3.1 1.0 1.0 CG B:ASN293 3.2 0.8 1.0 PA B:ACP401 3.2 0.7 1.0 O3A B:ACP401 3.2 0.8 1.0 CD B:GLU289 3.3 0.7 1.0 PG B:ACP401 3.3 0.6 1.0 O1G B:ACP401 3.4 0.1 1.0 ND2 B:ASN293 3.6 0.8 1.0 OE1 B:GLU289 3.7 0.8 1.0 C3B B:ACP401 3.7 0.8 1.0 NE2 B:HIS297 4.2 0.3 1.0 O5' B:ACP401 4.2 0.7 1.0 NZ B:LYS296 4.2 0.5 1.0 CE B:LYS296 4.2 0.8 1.0 O2A B:ACP401 4.3 0.2 1.0 N B:GLY336 4.4 0.2 1.0 O2B B:ACP401 4.4 0.3 1.0 CA B:GLY336 4.4 0.3 1.0 CB B:ASN293 4.5 0.1 1.0 CG B:GLU289 4.6 0.0 1.0 O2G B:ACP401 4.7 0.3 1.0 CA B:ASN293 4.8 0.7 1.0 CD2 B:HIS297 4.9 0.6 1.0

F.Trajtenberg, J.A.Imelio, M.R.Machado, N.Larrieux, M.A.Marti, G.Obal, A.E.Mechaly, A.Buschiazzo. Regulation of Signaling Directionality Revealed By 3D Snapshots of A Kinase:Regulator Complex in Action. Elife V. 5 2016.
ISSN: ESSN 2050-084X
PubMed: 27938660
DOI: 10.7554/ELIFE.21422