Magnesium in PDB 7jus: Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

All present enzymatic activity of Crystal Structure of KSR2: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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib, PDB code: 7jus 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)	46.72 / 2.99
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	140.000, 140.000, 220.000, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 26.5

The structure of Crystal Structure of KSR2: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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib (pdb code 7jus). 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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib, PDB code: 7jus:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of KSR2: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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:72.7 occ:1.00 O2A B:ANP1001 2.1 78.5 1.0 O2B B:ANP1001 2.1 93.4 1.0 OD1 B:ASP803 2.2 85.7 1.0 O B:HOH1102 2.2 80.8 1.0 OD1 B:ASN791 2.3 69.5 1.0 O B:HOH1104 2.4 78.2 1.0 CG B:ASN791 3.3 68.8 1.0 PA B:ANP1001 3.3 87.9 1.0 PB B:ANP1001 3.3 86.0 1.0 CG B:ASP803 3.4 84.9 1.0 O3A B:ANP1001 3.5 0.3 1.0 O2G B:ANP1001 3.6 93.9 1.0 ND2 B:ASN791 3.6 62.9 1.0 CB B:ASP803 4.0 70.1 1.0 NH2 B:ARG692 4.2 83.0 1.0 O5' B:ANP1001 4.2 76.2 1.0 O1B B:ANP1001 4.3 85.8 1.0 OD2 B:ASP803 4.4 93.0 1.0 N3B B:ANP1001 4.4 79.6 1.0 O1A B:ANP1001 4.4 89.6 1.0 O B:LYS790 4.5 82.8 1.0 CB B:ASN791 4.6 63.4 1.0 PG B:ANP1001 4.6 88.8 1.0 CA B:ASN791 4.9 69.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of KSR2: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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg503 b:0.4 occ:1.00 O1A C:ANP502 2.1 0.4 1.0 O3G C:ANP502 2.2 0.7 1.0 O1B C:ANP502 2.3 0.8 1.0 O2G C:ANP502 2.4 0.4 1.0 ND2 C:ASN195 2.5 0.1 1.0 PG C:ANP502 2.7 0.5 1.0 O3A C:ANP502 2.7 0.1 1.0 OD1 C:ASP208 2.7 0.6 1.0 PA C:ANP502 2.8 0.6 1.0 PB C:ANP502 2.9 0.3 1.0 OD1 C:ASN195 3.0 0.6 1.0 CG C:ASN195 3.1 0.2 1.0 NZ C:LYS97 3.1 0.9 1.0 N3B C:ANP502 3.3 0.5 1.0 CG C:ASP208 3.6 0.8 1.0 O5' C:ANP502 3.8 0.9 1.0 O1G C:ANP502 4.0 1.0 1.0 O2A C:ANP502 4.0 0.8 1.0 C21 C:VKD501 4.1 0.3 1.0 O2B C:ANP502 4.3 0.3 1.0 CE C:LYS97 4.4 0.6 1.0 CB C:ASP208 4.4 0.4 1.0 OD2 C:ASP208 4.4 0.1 1.0 OG C:SER194 4.6 0.8 1.0 CB C:ASN195 4.6 1.0 1.0 O C:SER194 4.9 0.3 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