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

All present enzymatic activity of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib:
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 Trametinib, PDB code: 7jur 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)	46.90 / 2.82
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	140.000, 140.000, 222.000, 90.00, 90.00, 120.00
R / Rfree (%)	23.7 / 27.7

The structure of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib also contains other interesting chemical elements:

Fluorine	(F)	1 atom
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 Trametinib (pdb code 7jur). 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 Trametinib, PDB code: 7jur:
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 Trametinib


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 Trametinib within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1002 b:47.9 occ:1.00 OD1 B:ASN791 2.1 46.5 1.0 O2B B:ANP1001 2.1 53.3 1.0 O2A B:ANP1001 2.2 35.9 1.0 OD1 B:ASP803 2.4 49.6 1.0 O B:HOH1101 2.7 41.2 1.0 PB B:ANP1001 3.2 49.7 1.0 CG B:ASN791 3.3 43.9 1.0 PA B:ANP1001 3.3 51.9 1.0 O B:LYS790 3.4 47.2 1.0 O1B B:ANP1001 3.4 46.0 1.0 CG B:ASP803 3.6 54.2 1.0 O3A B:ANP1001 3.7 56.9 1.0 O5' B:ANP1001 3.8 45.0 1.0 ND2 B:ASN791 4.1 42.0 1.0 C B:LYS790 4.2 45.9 1.0 CA B:ASN791 4.3 45.0 1.0 CB B:ASN791 4.3 42.9 1.0 OD2 B:ASP803 4.4 54.6 1.0 OG1 B:THR802 4.4 46.6 1.0 O2G B:ANP1001 4.4 59.0 1.0 CB B:ASP803 4.5 44.4 1.0 N B:ASN791 4.6 47.3 1.0 NH2 B:ARG692 4.6 50.6 1.0 O1A B:ANP1001 4.7 48.9 1.0 N3B B:ANP1001 4.7 33.0 1.0 C2' B:ANP1001 4.7 47.5 1.0 C8 B:ANP1001 4.8 47.8 1.0 CB B:LYS790 4.9 47.4 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 Trametinib


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 Trametinib within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg403 b:93.4 occ:1.00 O3G C:ANP401 2.0 0.4 1.0 ND2 C:ASN195 2.0 0.9 1.0 O1A C:ANP401 2.0 98.5 1.0 OD1 C:ASP208 2.0 95.5 1.0 CG C:ASP208 3.0 94.8 1.0 CG C:ASN195 3.1 98.2 1.0 PA C:ANP401 3.4 0.9 1.0 OD1 C:ASN195 3.5 0.8 1.0 PG C:ANP401 3.5 0.4 1.0 O1B C:ANP401 3.6 0.9 1.0 OD2 C:ASP208 3.8 98.6 1.0 CB C:ASP208 3.9 90.5 1.0 NZ C:LYS97 3.9 91.5 1.0 O5' C:ANP401 4.0 0.8 1.0 O3A C:ANP401 4.0 0.1 1.0 O2G C:ANP401 4.1 0.2 1.0 PB C:ANP401 4.3 0.7 1.0 O1G C:ANP401 4.3 0.3 1.0 CB C:ASN195 4.3 90.3 1.0 O C:SER194 4.4 95.9 1.0 O2A C:ANP401 4.5 0.9 1.0 C37 C:QOM402 4.5 0.2 1.0 N3B C:ANP401 4.5 0.1 1.0 CA C:ASN195 4.7 87.5 1.0 C35 C:QOM402 4.7 0.4 1.0 C C:SER194 4.9 85.9 1.0 C8 C:ANP401 5.0 1.0 1.0 OG C:SER194 5.0 97.9 1.0 SG C:CYS207 5.0 0.2 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