Iodine in PDB 4mne: Crystal Structure of the Braf:MEK1 Complex

All present enzymatic activity of Crystal Structure of the Braf:MEK1 Complex:
2.7.11.1; 2.7.12.2;

The structure of Crystal Structure of the Braf:MEK1 Complex, PDB code: 4mne was solved by J.Sudhamsu, J.R.Haling, T.Morales, B.Brandhuber, S.G.Hymowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.59 / 2.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	97.498, 135.657, 256.059, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 24

The structure of Crystal Structure of the Braf:MEK1 Complex also contains other interesting chemical elements:

Fluorine	(F)	10 atoms
Magnesium	(Mg)	4 atoms
Chlorine	(Cl)	1 atom

The binding sites of Iodine atom in the Crystal Structure of the Braf:MEK1 Complex (pdb code 4mne). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 5 binding sites of Iodine where determined in the Crystal Structure of the Braf:MEK1 Complex, PDB code: 4mne:
Jump to Iodine binding site number: 1; 2; 3; 4; 5;

Iodine binding site 1 out of 5 in the Crystal Structure of the Braf:MEK1 Complex


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 the Braf:MEK1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:I903 b:46.0 occ:1.00 I27 A:573903 0.0 46.0 1.0 C23 A:573903 2.1 51.9 1.0 C24 A:573903 3.1 44.5 1.0 C22 A:573903 3.1 43.5 1.0 O A:VAL127 3.4 29.0 1.0 CE2 A:PHE209 4.1 44.2 1.0 C A:VAL127 4.1 32.2 1.0 CZ A:PHE209 4.2 43.8 1.0 CB A:VAL127 4.3 28.1 1.0 SG A:CYS207 4.3 28.9 0.5 C25 A:573903 4.4 41.5 1.0 C21 A:573903 4.4 41.8 1.0 CG1 A:VAL127 4.4 27.1 1.0 CD1 A:LEU118 4.4 43.8 1.0 O A:GLY128 4.5 36.4 1.0 CD2 A:LEU118 4.6 46.8 1.0 CA A:VAL127 4.7 33.8 1.0 C A:GLY128 4.7 38.7 1.0 CB A:MET143 4.8 35.6 1.0 CA A:CYS207 4.9 34.7 0.5 CB A:PHE129 4.9 31.4 1.0 SD A:MET143 4.9 44.6 1.0 C20 A:573903 4.9 43.9 1.0 CA A:CYS207 4.9 34.7 0.5 CB A:CYS207 4.9 33.0 0.5 N A:GLY128 5.0 36.1 1.0 N A:VAL127 5.0 32.5 1.0 CD2 A:PHE209 5.0 39.4 1.0

Iodine binding site 2 out of 5 in the Crystal Structure of the Braf:MEK1 Complex


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Crystal Structure of the Braf:MEK1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:I903 b:37.8 occ:1.00 I27 D:573903 0.0 37.8 1.0 C23 D:573903 2.1 42.0 1.0 C24 D:573903 3.0 35.6 1.0 C22 D:573903 3.1 33.8 1.0 O D:VAL127 3.4 26.2 1.0 CE2 D:PHE209 4.0 23.9 1.0 CG1 D:VAL127 4.0 27.5 1.0 CB D:VAL127 4.1 31.9 1.0 CZ D:PHE209 4.2 27.0 1.0 C D:VAL127 4.2 28.5 1.0 CD2 D:LEU118 4.3 32.8 1.0 O D:GLY128 4.3 29.6 1.0 C25 D:573903 4.4 38.4 1.0 C21 D:573903 4.4 37.2 1.0 CB D:PHE129 4.5 31.3 1.0 SG D:CYS207 4.7 54.3 1.0 C D:GLY128 4.7 27.0 1.0 CA D:VAL127 4.7 29.3 1.0 CD1 D:LEU118 4.7 31.2 1.0 CG2 D:ILE126 4.9 33.0 1.0 C20 D:573903 4.9 42.0 1.0 CB D:MET143 5.0 33.4 1.0 CD2 D:PHE209 5.0 28.2 1.0 N D:PHE129 5.0 31.3 1.0

Iodine binding site 3 out of 5 in the Crystal Structure of the Braf:MEK1 Complex


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of Crystal Structure of the Braf:MEK1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:I903 b:55.3 occ:1.00 I27 E:573903 0.0 55.3 1.0 C23 E:573903 2.1 54.3 1.0 C24 E:573903 3.0 47.1 1.0 C22 E:573903 3.1 48.6 1.0 O E:VAL127 3.5 32.4 1.0 SG E:CYS207 3.9 36.8 0.5 CE2 E:PHE209 3.9 41.4 1.0 CB E:VAL127 4.0 36.0 1.0 CZ E:PHE209 4.1 43.9 1.0 C E:VAL127 4.2 39.6 1.0 C25 E:573903 4.3 47.6 1.0 C21 E:573903 4.4 47.6 1.0 CG1 E:VAL127 4.4 34.9 1.0 CA E:VAL127 4.5 36.8 1.0 CD1 E:LEU118 4.6 55.1 1.0 CB E:CYS207 4.7 40.7 0.5 O E:GLY128 4.7 48.7 1.0 SD E:MET143 4.7 51.0 1.0 CB E:MET143 4.8 54.9 1.0 N E:VAL127 4.8 37.7 1.0 CD2 E:PHE209 4.9 44.8 1.0 CA E:CYS207 4.9 41.7 0.5 CD2 E:LEU118 4.9 58.3 1.0 C20 E:573903 4.9 47.7 1.0 CA E:CYS207 4.9 41.7 0.5 CG2 E:ILE126 4.9 45.1 1.0 C E:GLY128 5.0 53.2 1.0 CB E:CYS207 5.0 40.7 0.5

Iodine binding site 4 out of 5 in the Crystal Structure of the Braf:MEK1 Complex


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 4 of Crystal Structure of the Braf:MEK1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ H:I903 b:43.1 occ:1.00 I27 H:573903 0.0 43.1 1.0 C23 H:573903 2.1 43.4 1.0 C24 H:573903 3.0 37.5 1.0 C22 H:573903 3.1 40.9 1.0 O H:VAL127 3.4 27.7 1.0 CG1 H:VAL127 3.7 37.1 1.0 CB H:VAL127 4.0 39.3 1.0 C H:VAL127 4.0 37.5 1.0 CE2 H:PHE209 4.0 34.3 1.0 CZ H:PHE209 4.1 34.9 1.0 CD1 H:LEU118 4.1 37.5 1.0 C25 H:573903 4.3 39.1 1.0 SG H:CYS207 4.3 50.5 1.0 O H:GLY128 4.3 32.0 1.0 C21 H:573903 4.4 40.9 1.0 CA H:VAL127 4.5 41.6 1.0 C H:GLY128 4.5 30.5 1.0 CD2 H:LEU118 4.8 39.5 1.0 CB H:PHE129 4.8 35.2 1.0 N H:PHE129 4.8 39.1 1.0 C20 H:573903 4.9 42.1 1.0 N H:GLY128 4.9 30.9 1.0 CB H:MET143 4.9 33.9 1.0 N H:VAL127 4.9 40.5 1.0 CG2 H:ILE126 4.9 41.4 1.0 CA H:PHE129 4.9 40.2 1.0 CG H:LEU118 5.0 38.1 1.0

Iodine binding site 5 out of 5 in the Crystal Structure of the Braf:MEK1 Complex


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 5 of Crystal Structure of the Braf:MEK1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ H:I904 b:61.8 occ:1.00 I27 H:573904 0.0 61.8 1.0 C23 H:573904 2.1 62.4 1.0 C24 H:573904 3.1 59.8 1.0 C22 H:573904 3.1 55.9 1.0 CG H:HIS87 3.5 58.2 1.0 CD2 H:HIS87 3.7 57.5 1.0 CB H:HIS87 3.7 53.2 1.0 ND1 H:HIS87 4.0 53.5 1.0 NE2 H:HIS87 4.2 60.3 1.0 SD H:MET94 4.4 41.7 1.0 CE2 H:PHE68 4.4 55.7 1.0 CE1 H:HIS87 4.4 56.6 1.0 CZ H:PHE68 4.4 58.5 1.0 C25 H:573904 4.4 56.0 1.0 C21 H:573904 4.4 44.8 1.0 CE H:MET94 4.5 41.8 1.0 CD1 H:LEU92 4.8 57.0 1.0 OG H:SER90 5.0 60.7 1.0 C20 H:573904 5.0 54.4 1.0

J.R.Haling, J.Sudhamsu, I.Yen, S.Sideris, W.Sandoval, W.Phung, B.J.Bravo, A.M.Giannetti, A.Peck, A.Masselot, T.Morales, D.Smith, B.J.Brandhuber, S.G.Hymowitz, S.Malek. Structure of the Braf-Mek Complex Reveals A Kinase Activity Independent Role For Braf in Mapk Signaling. Cancer Cell V. 26 402 2014.
ISSN: ISSN 1535-6108
PubMed: 25155755
DOI: 10.1016/J.CCR.2014.07.007