Magnesium in PDB 7juq: Crystal Structure of KSR2:MEK1 in Complex with Adp

All present enzymatic activity of Crystal Structure of KSR2:MEK1 in Complex with Adp:
2.7.11.1; 2.7.12.2;

The structure of Crystal Structure of KSR2:MEK1 in Complex with Adp, PDB code: 7juq was solved by Z.M.Khan, A.C.Dar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.50 / 3.22
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	139.000, 139.000, 222.000, 90.00, 90.00, 120.00
R / Rfree (%)	25.4 / 28.8

The binding sites of Magnesium atom in the Crystal Structure of KSR2:MEK1 in Complex with Adp (pdb code 7juq). 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 KSR2:MEK1 in Complex with Adp, PDB code: 7juq:

Magnesium binding site 1 out of 1 in the Crystal Structure of KSR2:MEK1 in Complex with Adp


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 KSR2:MEK1 in Complex with Adp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:0.2 occ:1.00 OD1 B:ASN791 2.0 90.2 1.0 O2A B:ADP1001 2.1 84.9 1.0 OD2 B:ASP803 2.1 96.2 1.0 CG B:ASN791 2.6 84.8 1.0 ND2 B:ASN791 2.7 82.0 1.0 CG B:ASP803 3.0 92.7 1.0 O1B B:ADP1001 3.1 0.5 1.0 CB B:ASP803 3.2 82.5 1.0 PA B:ADP1001 3.3 0.3 1.0 O1A B:ADP1001 3.9 96.2 1.0 CB B:ASN791 3.9 64.5 1.0 O3A B:ADP1001 4.0 0.0 1.0 OD1 B:ASP803 4.2 0.2 1.0 PB B:ADP1001 4.2 0.7 1.0 NH1 B:ARG692 4.2 94.4 1.0 OD2 B:ASP786 4.5 96.1 1.0 O5' B:ADP1001 4.5 93.8 1.0 CA B:ASN791 4.6 78.5 1.0 CA B:ASP803 4.7 80.7 1.0 CE B:LYS788 4.8 74.5 1.0 O B:LYS790 4.9 92.8 1.0 O2B B:ADP1001 4.9 76.7 1.0 O B:THR802 5.0 86.2 1.0

Z.M.Khan, A.M.Real, W.M.Marsiglia, A.Chow, M.E.Duffy, J.R.Yerabolu, A.P.Scopton, A.C.Dar. Structural Basis For the Action of the Drug Trametinib at Ksr-Bound Mek. Nature 2020.
ISSN: ESSN 1476-4687
PubMed: 32927473
DOI: 10.1038/S41586-020-2760-4