Magnesium in PDB 7juy: Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

All present enzymatic activity of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib:
2.7.11.1; 2.7.12.2;

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib, PDB code: 7juy 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)	49.65 / 3.10
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	136.000, 136.000, 219.000, 90.00, 90.00, 120.00
R / Rfree (%)	24.7 / 25.7

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Iodine	(I)	1 atom

The binding sites of Magnesium atom in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib (pdb code 7juy). 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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib, PDB code: 7juy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib


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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg902 b:99.1 occ:1.00 O1A B:ANP901 2.2 0.8 1.0 O2G B:ANP901 2.5 0.6 1.0 O1B B:ANP901 2.5 0.9 1.0 OD1 B:ASN738 3.2 83.5 1.0 OD2 B:ASP750 3.2 93.3 1.0 ND2 B:ASN738 3.3 80.0 1.0 OD2 B:ASP733 3.4 93.7 1.0 PA B:ANP901 3.6 0.9 1.0 CG B:ASN738 3.7 81.6 1.0 PB B:ANP901 3.7 0.2 1.0 PG B:ANP901 3.8 0.9 1.0 CG B:ASP750 3.8 85.6 1.0 CB B:ASP750 4.0 83.7 1.0 O B:HOH1001 4.0 91.6 1.0 O3A B:ANP901 4.1 0.3 1.0 O3G B:ANP901 4.2 0.6 1.0 NZ B:LYS735 4.2 94.1 1.0 CE B:LYS735 4.2 85.6 1.0 N3B B:ANP901 4.3 0.6 1.0 O5' B:ANP901 4.3 0.4 1.0 CG B:ASP733 4.6 89.5 1.0 NH2 B:ARG639 4.7 91.3 1.0 O2A B:ANP901 4.7 97.6 1.0 OD1 B:ASP750 4.7 87.3 1.0 O2B B:ANP901 4.9 0.1 1.0 O1G B:ANP901 5.0 0.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib


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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg403 b:0.2 occ:1.00 O1A C:ANP401 2.2 0.1 1.0 OD2 C:ASP208 2.3 0.6 1.0 OD1 C:ASN195 2.5 0.7 1.0 O1B C:ANP401 2.8 0.6 1.0 O3G C:ANP401 3.0 0.1 1.0 CG C:ASP208 3.2 0.5 1.0 CG C:ASN195 3.5 0.5 1.0 PA C:ANP401 3.5 0.7 1.0 SG C:CYS207 3.6 0.1 1.0 O C:SER194 3.6 0.6 1.0 OD1 C:ASP208 3.8 0.7 1.0 C8 C:ANP401 3.9 0.3 1.0 O5' C:ANP401 4.0 0.4 1.0 PB C:ANP401 4.0 0.8 1.0 CB C:ASP208 4.0 1.0 1.0 O3A C:ANP401 4.2 0.7 1.0 NZ C:LYS97 4.2 0.1 1.0 PG C:ANP401 4.2 0.6 1.0 ND2 C:ASN195 4.2 0.0 1.0 N7 C:ANP401 4.3 0.4 1.0 CA C:ASN195 4.4 0.1 1.0 CB C:ASN195 4.5 0.5 1.0 N3B C:ANP401 4.5 0.0 1.0 C C:SER194 4.5 0.6 1.0 O1G C:ANP401 4.6 0.4 1.0 OG C:SER194 4.6 0.3 1.0 O24 C:EUI402 4.6 0.3 1.0 O2A C:ANP401 4.8 0.9 1.0 N C:ASN195 4.8 0.6 1.0 C21 C:EUI402 4.9 0.5 1.0 C2' C:ANP401 4.9 0.7 1.0 N9 C:ANP401 5.0 0.8 1.0 CB C:CYS207 5.0 0.1 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