Iodine in PDB 5ax3: Crystal Structure of ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors.

All present enzymatic activity of Crystal Structure of ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors.:
2.7.11.24;

The structure of Crystal Structure of ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors., PDB code: 5ax3 was solved by T.Kinoshita, H.Sugiyama, Y.Mori, N.Takahashi, A.Tomonaga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.89 / 2.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.835, 66.465, 116.871, 90.00, 90.00, 90.00
R / Rfree (%)	23.6 / 28.5

The binding sites of Iodine atom in the Crystal Structure of ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors. (pdb code 5ax3). 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 ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors., PDB code: 5ax3:

Iodine binding site 1 out of 1 in the Crystal Structure of ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors.


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 ERK2 Complexed with Allosteric and Atp- Competitive Inhibitors. within 5.0Å range: probe atom residue distance (Å) B Occ A:I401 b:0.1 occ:1.00 IAE A:5ID401 0.0 0.1 1.0 C7 A:5ID401 2.1 95.6 1.0 C8 A:5ID401 3.1 85.3 1.0 C5 A:5ID401 3.2 83.8 1.0 N6 A:5ID401 3.4 71.5 1.0 C6 A:5ID401 3.8 83.3 1.0 NE2 A:GLN96 3.8 54.3 1.0 CD A:GLN96 4.3 53.9 1.0 N9 A:5ID401 4.3 75.8 1.0 C4 A:5ID401 4.3 74.9 1.0 CD A:LYS45 4.4 93.3 1.0 OE1 A:GLN96 4.4 75.6 1.0 CD1 A:LEU147 4.4 65.6 1.0 SG A:CYS157 4.6 0.7 1.0 CE A:LYS45 5.0 76.9 1.0

T.Kinoshita, H.Sugiyama, Y.Mori, N.Takahashi, A.Tomonaga. Identification of Allosteric ERK2 Inhibitors Through in Silico Biased Screening and Competitive Binding Assay Bioorg.Med.Chem.Lett. V. 26 955 2016.
ISSN: ESSN 1464-3405
PubMed: 26733474
DOI: 10.1016/J.BMCL.2015.12.056