Iodine in PDB 4lmn: Crystal Structure of MEK1 Kinase Bound to GDC0973

All present enzymatic activity of Crystal Structure of MEK1 Kinase Bound to GDC0973:
2.7.12.2;

The structure of Crystal Structure of MEK1 Kinase Bound to GDC0973, PDB code: 4lmn was solved by M.H.Ultsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.69 / 2.80
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	81.610, 81.610, 129.809, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 23.3

The structure of Crystal Structure of MEK1 Kinase Bound to GDC0973 also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Magnesium	(Mg)	1 atom

The binding sites of Iodine atom in the Crystal Structure of MEK1 Kinase Bound to GDC0973 (pdb code 4lmn). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total only one binding site of Iodine was determined in the Crystal Structure of MEK1 Kinase Bound to GDC0973, PDB code: 4lmn:

Iodine binding site 1 out of 1 in the Crystal Structure of MEK1 Kinase Bound to GDC0973


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure of MEK1 Kinase Bound to GDC0973 within 5.0Å range: probe atom residue distance (Å) B Occ A:I503 b:67.8 occ:1.00 I8 A:EUI503 0.0 67.8 1.0 C2 A:EUI503 2.1 72.6 1.0 C3 A:EUI503 3.1 70.6 1.0 C1 A:EUI503 3.1 72.2 1.0 O A:VAL127 3.3 58.8 1.0 CZ A:PHE209 4.0 60.2 1.0 CE2 A:PHE209 4.0 61.3 1.0 CB A:VAL127 4.1 57.0 1.0 C A:VAL127 4.1 60.2 1.0 CG1 A:VAL127 4.3 56.5 1.0 C4 A:EUI503 4.4 68.8 1.0 C6 A:EUI503 4.4 70.7 1.0 CB A:CYS207 4.4 69.2 1.0 O A:GLY128 4.4 63.9 1.0 CA A:VAL127 4.5 56.6 1.0 CD2 A:LEU118 4.5 69.5 1.0 CA A:CYS207 4.6 66.7 1.0 CB A:MET143 4.7 60.8 1.0 CD1 A:LEU118 4.8 67.8 1.0 C A:GLY128 4.8 63.8 1.0 CB A:PHE129 4.8 60.6 1.0 N A:VAL127 4.8 58.1 1.0 SD A:MET143 4.8 66.3 1.0 O A:LEU206 4.8 66.8 1.0 C5 A:EUI503 4.9 69.3 1.0 CG2 A:ILE126 5.0 60.3 1.0 CE1 A:PHE209 5.0 60.5 1.0

G.Hatzivassiliou, J.R.Haling, H.Chen, K.Song, S.Price, R.Heald, J.F.Hewitt, M.Zak, A.Peck, C.Orr, M.Merchant, K.P.Hoeflich, J.Chan, S.M.Luoh, D.J.Anderson, M.J.Ludlam, C.Wiesmann, M.Ultsch, L.S.Friedman, S.Malek, M.Belvin. Mechanism of Mek Inhibition Determines Efficacy in Mutant Kras- Versus Braf-Driven Cancers. Nature V. 501 232 2013.
ISSN: ISSN 0028-0836
PubMed: 23934108
DOI: 10.1038/NATURE12441