Chlorine in PDB 5e4a: Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid.

The structure of Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid., PDB code: 5e4a was solved by L.Ciccone, S.Nencetti, A.Rossello, E.Orlandini, E.A.Stura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.99 / 1.33
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	43.210, 85.990, 63.820, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 19.2

The binding sites of Chlorine atom in the Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid. (pdb code 5e4a). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid., PDB code: 5e4a:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:29.9 occ:0.47 CL1 A:5JW201 0.0 29.9 0.5 C16 A:5JW201 1.8 29.5 0.5 C15 A:5JW201 2.7 26.5 0.5 C17 A:5JW201 2.8 34.2 0.5 C13 A:5JW201 4.0 27.8 0.5 C18 A:5JW201 4.1 30.4 0.5 CD1 A:LEU17 4.2 23.3 1.0 C12 A:5JW201 4.5 28.3 0.5

Chlorine binding site 2 out of 2 in the Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Transthyretin (Ttr) Complexed with (2,7-Dichloro-Fluoren-9- Ylideneaminooxy)-Acetic Acid. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:36.0 occ:0.47 CL2 A:5JW201 0.0 36.0 0.5 C05 A:5JW201 1.8 33.6 0.5 C06 A:5JW201 2.8 34.9 0.5 C04 A:5JW201 2.8 28.4 0.5 CG2 A:VAL121 3.4 20.2 1.0 CB A:ALA108 3.6 17.4 1.0 O A:THR119 3.7 13.3 0.5 CG2 A:THR119 3.8 26.2 0.5 O A:THR106 3.9 14.1 1.0 CB A:VAL121 3.9 15.7 1.0 N A:VAL121 3.9 13.0 1.0 CG2 A:THR106 3.9 17.6 1.0 C03 A:5JW201 4.1 31.7 0.5 C01 A:5JW201 4.1 33.7 0.5 CG2 A:THR119 4.2 11.9 0.6 N A:ALA108 4.2 14.2 1.0 CB A:THR106 4.3 14.5 1.0 C A:THR119 4.4 12.8 0.5 O A:THR119 4.4 10.8 0.6 C A:ALA120 4.4 13.4 1.0 C A:THR106 4.4 12.3 1.0 CA A:ALA108 4.5 14.1 1.0 CA A:VAL121 4.5 14.1 1.0 C A:THR119 4.6 9.5 0.6 C02 A:5JW201 4.6 33.3 0.5 CA A:ALA120 4.6 12.6 1.0 CB A:THR119 4.6 10.3 0.6 N A:ALA120 4.8 12.0 1.0 CB A:THR119 5.0 18.0 0.5 C A:ILE107 5.0 12.9 1.0

L.Ciccone, S.Nencetti, A.Rossello, E.A.Stura, E.Orlandini. Synthesis and Structural Analysis of Halogen Substituted Fibril Formation Inhibitors of Human Transthyretin (Ttr). J Enzyme Inhib Med Chem V. 31 40 2016.
ISSN: ESSN 1475-6374
PubMed: 27067161
DOI: 10.3109/14756366.2016.1167048