Iodine in PDB 2zoq: Structural Dissection of Human Mitogen-Activated Kinase ERK1

All present enzymatic activity of Structural Dissection of Human Mitogen-Activated Kinase ERK1:
2.7.11.24;

The structure of Structural Dissection of Human Mitogen-Activated Kinase ERK1, PDB code: 2zoq was solved by T.Kinoshita, T.Tada, S.Nakae, I.Yoshida, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.57 / 2.39
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.382, 91.540, 64.930, 90.00, 91.50, 90.00
R / Rfree (%)	n/a / n/a

The structure of Structural Dissection of Human Mitogen-Activated Kinase ERK1 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Iodine atom in the Structural Dissection of Human Mitogen-Activated Kinase ERK1 (pdb code 2zoq). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the Structural Dissection of Human Mitogen-Activated Kinase ERK1, PDB code: 2zoq:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in the Structural Dissection of Human Mitogen-Activated Kinase ERK1


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Structural Dissection of Human Mitogen-Activated Kinase ERK1 within 5.0Å range: probe atom residue distance (Å) B Occ A:I382 b:38.9 occ:1.00 IAE A:5ID382 0.0 38.9 1.0 C7 A:5ID382 2.1 30.4 1.0 NA A:NA381 2.7 41.8 1.0 OE1 A:GLN122 2.9 17.4 1.0 C8 A:5ID382 3.1 28.1 1.0 C5 A:5ID382 3.2 29.2 1.0 O A:HOH389 3.5 11.0 1.0 CD A:GLN122 3.6 14.0 1.0 N6 A:5ID382 3.7 28.3 1.0 NE2 A:GLN122 3.8 19.8 1.0 C6 A:5ID382 3.9 28.0 1.0 SG A:CYS183 4.2 15.4 1.0 CD1 A:LEU173 4.2 7.5 1.0 N9 A:5ID382 4.3 26.3 1.0 C4 A:5ID382 4.3 27.3 1.0 CG1 A:VAL56 4.5 25.1 1.0 OD1 A:ASP184 4.7 20.5 1.0 CG A:GLN122 4.8 14.7 1.0 CB A:GLN122 4.8 11.0 1.0 CE A:LYS71 4.9 17.5 1.0

Iodine binding site 2 out of 2 in the Structural Dissection of Human Mitogen-Activated Kinase ERK1


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Structural Dissection of Human Mitogen-Activated Kinase ERK1 within 5.0Å range: probe atom residue distance (Å) B Occ B:I382 b:33.0 occ:1.00 IAE B:5ID382 0.0 33.0 1.0 C7 B:5ID382 2.0 25.6 1.0 NA B:NA381 2.9 33.0 1.0 C8 B:5ID382 3.0 25.2 1.0 C5 B:5ID382 3.1 25.6 1.0 OE1 B:GLN122 3.2 13.1 1.0 O B:HOH432 3.4 13.3 1.0 N6 B:5ID382 3.7 23.2 1.0 CD B:GLN122 3.7 12.7 1.0 NE2 B:GLN122 3.8 16.8 1.0 C6 B:5ID382 3.8 25.9 1.0 N9 B:5ID382 4.2 24.7 1.0 C4 B:5ID382 4.2 26.5 1.0 CB B:CYS183 4.3 14.2 1.0 CD2 B:LEU173 4.6 13.3 1.0 SG B:CYS183 4.6 11.1 1.0 CE B:LYS71 4.7 18.8 1.0 CB B:GLN122 4.7 15.2 1.0 CG B:GLN122 4.8 15.4 1.0 OD1 B:ASP184 5.0 19.9 1.0

T.Kinoshita, I.Yoshida, S.Nakae, K.Okita, M.Gouda, M.Matsubara, K.Yokota, H.Ishiguro, T.Tada. Crystal Structure of Human Mono-Phosphorylated ERK1 at TYR204 Biochem.Biophys.Res.Commun. V. 377 1123 2008.
ISSN: ISSN 0006-291X
PubMed: 18983981
DOI: 10.1016/J.BBRC.2008.10.127