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Magnesium in PDB 7jv0: Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901

Enzymatic activity of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901

All present enzymatic activity of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901:
2.7.11.1; 2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901, PDB code: 7jv0 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) 40.00 / 3.63
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 137.660, 137.660, 220.890, 90.00, 90.00, 120.00
R / Rfree (%) 24.6 / 26

Other elements in 7jv0:

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901 also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901 (pdb code 7jv0). 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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901, PDB code: 7jv0:

Magnesium binding site 1 out of 1 in 7jv0

Go back to Magnesium Binding Sites List in 7jv0
Magnesium binding site 1 out of 1 in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor PD0325901


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 PD0325901 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:0.7
occ:1.00
 O2G A:ANP901 2.1 0.1 1.0
OD2 A:ASP733 2.9 0.6 1.0
O1A A:ANP901 3.1 0.4 1.0
PG A:ANP901 3.7 0.4 1.0
ND2 A:ASN738 3.7 0.4 1.0
O1B A:ANP901 3.8 0.8 1.0
NZ A:LYS735 3.8 0.8 1.0
CB A:ASP750 3.8 0.7 1.0
OD2 A:ASP750 3.9 0.4 1.0
CG A:ASP750 4.0 0.5 1.0
CG A:ASP733 4.1 0.4 1.0
CD2 A:LEU753 4.2 0.5 1.0
CE2 A:PHE754 4.3 0.6 1.0
PA A:ANP901 4.3 0.9 1.0
N3B A:ANP901 4.4 0.9 1.0
O3G A:ANP901 4.5 0.4 1.0
CD1 A:TRP624 4.5 0.5 1.0
PB A:ANP901 4.5 0.4 1.0
O1G A:ANP901 4.5 0.7 1.0
CG A:ASN738 4.6 99.9 1.0
OD1 A:ASN738 4.6 0.9 1.0
OD1 A:ASP750 4.6 0.4 1.0
O2A A:ANP901 4.7 0.4 1.0
O3A A:ANP901 4.7 0.2 1.0
O A:ASP750 4.7 97.0 1.0
NH2 A:ARG639 4.7 0.3 1.0
CB A:ASP733 4.9 0.8 1.0
OD1 A:ASP733 4.9 0.6 1.0
NH1 A:ARG639 4.9 0.8 1.0
NE1 A:TRP624 4.9 0.8 1.0

Reference:

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
Page generated: Wed Oct 2 22:00:55 2024

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