Magnesium in PDB 2y4i: KSR2-MEK1 Heterodimer

All present enzymatic activity of KSR2-MEK1 Heterodimer:
2.7.12.2;

The structure of KSR2-MEK1 Heterodimer, PDB code: 2y4i was solved by D.F.Brennan, D.Barford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.86 / 3.46
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	130.565, 130.565, 221.005, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 29.3

The structure of KSR2-MEK1 Heterodimer also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the KSR2-MEK1 Heterodimer (pdb code 2y4i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the KSR2-MEK1 Heterodimer, PDB code: 2y4i:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the KSR2-MEK1 Heterodimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of KSR2-MEK1 Heterodimer within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1933 b:95.0 occ:1.00 OD2 B:ASP803 2.5 0.1 1.0 O2A B:ATP1932 2.6 0.7 1.0 OD1 B:ASN791 2.6 0.4 1.0 O1B B:ATP1932 2.7 99.5 1.0 ND2 B:ASN791 3.2 0.5 1.0 O3B B:ATP1932 3.2 0.6 1.0 PB B:ATP1932 3.2 0.7 1.0 CG B:ASN791 3.3 0.6 1.0 O3A B:ATP1932 3.3 0.1 1.0 PA B:ATP1932 3.4 1.0 1.0 CG B:ASP803 3.4 0.3 1.0 CB B:ASP803 3.7 0.8 1.0 O3G B:ATP1932 4.0 0.4 1.0 O1A B:ATP1932 4.0 96.0 1.0 NH2 B:ARG692 4.0 0.8 1.0 PG B:ATP1932 4.3 1.0 1.0 OD1 B:ASP803 4.5 0.7 1.0 OD2 B:ASP786 4.7 0.9 1.0 CB B:ASN791 4.7 0.3 1.0 O2B B:ATP1932 4.8 0.9 1.0 O5' B:ATP1932 4.8 0.7 1.0

Magnesium binding site 2 out of 2 in the KSR2-MEK1 Heterodimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of KSR2-MEK1 Heterodimer within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1383 b:0.5 occ:1.00 O C:SER194 2.7 0.7 1.0 OD2 C:ASP208 2.8 0.6 1.0 O1B C:ATP1382 2.8 0.1 1.0 OD1 C:ASN195 2.9 0.6 1.0 O2A C:ATP1382 3.0 0.1 1.0 CG C:ASP208 3.2 0.3 1.0 OD1 C:ASP208 3.3 0.2 1.0 SG C:CYS207 3.4 0.6 1.0 C5' C:ATP1382 3.5 0.9 1.0 C8 C:ATP1382 3.7 0.4 1.0 C C:SER194 3.8 0.8 1.0 O5' C:ATP1382 3.9 0.1 1.0 CG C:ASN195 4.0 0.6 1.0 CA C:ASN195 4.0 0.8 1.0 PA C:ATP1382 4.0 0.2 1.0 PB C:ATP1382 4.1 0.8 1.0 C3' C:ATP1382 4.2 0.3 1.0 N7 C:ATP1382 4.3 0.6 1.0 C4' C:ATP1382 4.3 0.7 1.0 N C:ASN195 4.4 0.8 1.0 C2' C:ATP1382 4.4 0.5 1.0 CB C:ASP208 4.4 0.1 1.0 N9 C:ATP1382 4.4 0.4 1.0 O4' C:ATP1382 4.5 0.1 1.0 NZ C:LYS97 4.5 1.0 1.0 CD2 C:LEU197 4.5 0.9 1.0 CB C:ASN195 4.6 0.4 1.0 O3A C:ATP1382 4.6 0.1 1.0 C1' C:ATP1382 4.7 0.3 1.0 O2B C:ATP1382 4.9 0.1 1.0 O3G C:ATP1382 5.0 0.4 1.0

D.F.Brennan, A.C.Dar, N.T.Hertz, W.Chao, A.L.Burlingame, K.M.Shokat, D.Barford. A Raf-Induced Allosteric Transition of Ksr Stimulates Ksr and Raf Phosphorylation of Mek Nature V. 472 366 2011.
ISSN: ISSN 0028-0836
PubMed: 21441910
DOI: 10.1038/NATURE09860