Bromine in PDB 3cn3: Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene

The structure of Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene, PDB code: 3cn3 was solved by S.Connelly, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.29 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.859, 84.874, 64.791, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21.6

The binding sites of Bromine atom in the Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene (pdb code 3cn3). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene, PDB code: 3cn3:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene within 5.0Å range: probe atom residue distance (Å) B Occ A:Br128 b:29.0 occ:0.50 BRAB A:LJ4128 0.0 29.0 0.5 CAL A:LJ4128 1.9 26.5 0.5 CAP A:LJ4128 2.8 26.2 0.5 CAI A:LJ4128 2.9 27.1 0.5 OAA A:LJ4128 3.0 24.4 0.5 CG2 A:THR106 4.0 14.6 1.0 CAM A:LJ4128 4.1 26.6 0.5 CAO A:LJ4128 4.2 26.7 0.5 O A:HOH163 4.3 27.1 1.0 CD A:LYS15 4.3 17.1 1.0 CB A:ALA108 4.4 13.4 1.0 CG2 A:VAL121 4.5 17.4 1.0 CAJ A:LJ4128 4.7 26.8 0.5 CB A:THR106 4.9 15.0 1.0

Bromine binding site 2 out of 4 in the Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene within 5.0Å range: probe atom residue distance (Å) B Occ A:Br128 b:29.6 occ:0.50 BRAC A:LJ4128 0.0 29.6 0.5 CAM A:LJ4128 1.9 26.6 0.5 CAP A:LJ4128 2.8 26.2 0.5 CAJ A:LJ4128 2.9 26.8 0.5 OAA A:LJ4128 3.0 24.4 0.5 CD1 A:LEU17 3.7 19.0 1.0 NZ A:LYS15 3.9 20.3 1.0 CAL A:LJ4128 4.1 26.5 0.5 CAO A:LJ4128 4.2 26.7 0.5 CE A:LYS15 4.5 19.8 1.0 CAI A:LJ4128 4.6 27.1 0.5 CG A:LEU17 4.7 14.2 1.0 CD2 A:LEU17 4.9 14.1 1.0

Bromine binding site 3 out of 4 in the Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene within 5.0Å range: probe atom residue distance (Å) B Occ B:Br128 b:29.5 occ:0.50 BRAB B:LJ4128 0.0 29.5 0.5 CAL B:LJ4128 1.9 24.8 0.5 CAP B:LJ4128 2.8 22.3 0.5 CAI B:LJ4128 2.9 23.6 0.5 OAA B:LJ4128 2.9 21.7 0.5 CG2 B:THR106 4.0 18.5 1.0 CG2 B:VAL121 4.0 18.6 1.0 CAM B:LJ4128 4.1 23.5 0.5 CAO B:LJ4128 4.2 23.6 0.5 CAJ B:LJ4128 4.6 22.8 0.5 CB B:ALA108 4.6 15.6 1.0 CD B:LYS15 4.7 20.1 1.0 CB B:VAL121 4.7 17.6 1.0 CB B:THR106 4.8 18.1 1.0

Bromine binding site 4 out of 4 in the Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Human Transthyretin (Ttr) in Complex with 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene within 5.0Å range: probe atom residue distance (Å) B Occ B:Br128 b:23.9 occ:0.50 BRAC B:LJ4128 0.0 23.9 0.5 CAM B:LJ4128 1.9 23.5 0.5 CAJ B:LJ4128 2.8 22.8 0.5 CAP B:LJ4128 2.9 22.3 0.5 OAA B:LJ4128 3.2 21.7 0.5 CD1 B:LEU17 3.8 21.2 1.0 O B:HOH178 3.9 37.9 1.0 NZ B:LYS15 4.0 23.3 1.0 CAO B:LJ4128 4.1 23.6 0.5 CAL B:LJ4128 4.1 24.8 0.5 CE B:LYS15 4.4 23.1 1.0 CAI B:LJ4128 4.6 23.6 0.5 CG B:LEU17 4.9 15.4 1.0 CD2 B:LEU17 5.0 16.6 1.0

S.M.Johnson, S.Connelly, I.A.Wilson, J.W.Kelly. Toward Optimization of the Linker Substructure Common to Transthyretin Amyloidogenesis Inhibitors Using Biochemical and Structural Studies. J.Med.Chem. V. 51 6348 2008.
ISSN: ISSN 0022-2623
PubMed: 18811132
DOI: 10.1021/JM800435S