Iodine in PDB 2yj8: Cathepsin L with A Nitrile Inhibitor

All present enzymatic activity of Cathepsin L with A Nitrile Inhibitor:
3.4.22.15;

The structure of Cathepsin L with A Nitrile Inhibitor, PDB code: 2yj8 was solved by D.W.Banner, J.M.Benz, W.Haap, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.78 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.975, 57.265, 76.218, 90.00, 90.00, 90.00
R / Rfree (%)	14.055 / 18.159

The structure of Cathepsin L with A Nitrile Inhibitor also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Iodine atom in the Cathepsin L with A Nitrile Inhibitor (pdb code 2yj8). 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 Cathepsin L with A Nitrile Inhibitor, PDB code: 2yj8:

Iodine binding site 1 out of 1 in the Cathepsin L with A Nitrile Inhibitor


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Cathepsin L with A Nitrile Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:I1221 b:30.5 occ:1.00 I30 A:YJ81221 0.0 30.5 1.0 C27 A:YJ81221 2.1 27.0 1.0 C26 A:YJ81221 3.0 22.8 1.0 C28 A:YJ81221 3.0 23.4 1.0 HA2 A:GLY68 3.0 17.3 1.0 H26 A:YJ81221 3.1 23.3 1.0 HG3 A:GLU63 3.1 25.5 0.5 O A:GLY61 3.1 22.0 1.0 H28 A:YJ81221 3.1 24.0 1.0 HE2 A:TYR72 3.3 19.2 1.0 HA A:ASN62 3.5 17.6 1.0 HG2 A:GLU63 3.6 23.2 0.5 HG A:LEU69 3.9 17.9 1.0 CG A:GLU63 3.9 25.1 0.5 CD A:GLU63 3.9 31.8 0.5 CA A:GLY68 4.0 17.5 1.0 HD2 A:TYR72 4.0 19.9 1.0 OE2 A:GLU63 4.0 40.0 0.5 CE2 A:TYR72 4.1 20.3 1.0 C A:GLY61 4.2 19.4 1.0 H A:GLU63 4.3 18.9 0.5 HB2 A:GLU63 4.3 21.2 0.5 HG3 A:GLU63 4.3 24.3 0.5 C25 A:YJ81221 4.3 21.5 1.0 H A:GLU63 4.3 18.6 0.5 C29 A:YJ81221 4.3 24.8 1.0 CG A:GLU63 4.4 24.4 0.5 CA A:ASN62 4.4 17.7 1.0 N A:GLY68 4.4 15.2 1.0 CD2 A:TYR72 4.5 20.1 1.0 OE1 A:GLU63 4.5 41.4 0.5 O A:GLY67 4.5 19.0 1.0 HB2 A:GLU63 4.5 23.6 0.5 N A:GLU63 4.6 18.5 0.5 C A:GLY68 4.6 15.6 1.0 N A:GLU63 4.6 18.9 0.5 HA3 A:GLY68 4.6 16.9 1.0 HG2 A:GLU63 4.6 25.3 0.5 CB A:GLU63 4.6 21.5 0.5 C A:GLY67 4.7 17.3 1.0 H A:LEU69 4.7 15.2 1.0 OD1 A:ASN62 4.7 16.3 1.0 N A:ASN62 4.7 19.4 1.0 C A:ASN62 4.7 18.3 1.0 H A:GLY68 4.8 16.5 1.0 N A:LEU69 4.8 14.9 1.0 CG A:LEU69 4.8 17.6 1.0 C24 A:YJ81221 4.8 20.6 1.0 CB A:GLU63 5.0 23.9 0.5

L.A.Hardegger, B.Kuhn, B.Spinnler, L.Anselm, R.Ecabert, M.Stihle, B.Gsell, R.Thoma, J.Diez, J.M.Benz, J.Plancher, G.Hartmann, Y.Isshiki, K.Morikami, N.Shimma, W.Haap, D.W.Banner, F.Diederich. Halogen Bonding at the Active Sites of Human Cathepsin L and MEK1 Kinase: Efficient Interactions in Different Environments. Chemmedchem V. 6 2048 2011.
ISSN: ISSN 1860-7179
PubMed: 21898833
DOI: 10.1002/CMDC.201100353