Bromine in PDB 3cn2: Human Transthyretin (Ttr) in Complex with 3,5-Dibromo-4- Hydroxybiphenyl

The structure of Human Transthyretin (Ttr) in Complex with 3,5-Dibromo-4- Hydroxybiphenyl, PDB code: 3cn2 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)	38.43 / 1.52
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	43.058, 85.215, 64.811, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 19.7

The binding sites of Bromine atom in the Human Transthyretin (Ttr) in Complex with 3,5-Dibromo-4- Hydroxybiphenyl (pdb code 3cn2). 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 3,5-Dibromo-4- Hydroxybiphenyl, PDB code: 3cn2:
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 3,5-Dibromo-4- Hydroxybiphenyl


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 3,5-Dibromo-4- Hydroxybiphenyl within 5.0Å range: probe atom residue distance (Å) B Occ A:Br128 b:32.0 occ:0.50 BRAB A:LJ3128 0.0 32.0 0.5 CAL A:LJ3128 1.9 25.3 0.5 CAK A:LJ3128 2.7 25.7 0.5 CAI A:LJ3128 2.9 25.8 0.5 OAA A:LJ3128 3.0 24.1 0.5 CD1 A:LEU17 3.6 17.3 1.0 CAM A:LJ3128 4.1 25.3 0.5 CAO A:LJ3128 4.2 24.0 0.5 CE A:LYS15 4.3 23.2 1.0 CAJ A:LJ3128 4.7 25.6 0.5 CG A:LEU17 4.8 12.6 1.0 CD2 A:LEU17 4.9 15.2 1.0

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


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 3,5-Dibromo-4- Hydroxybiphenyl within 5.0Å range: probe atom residue distance (Å) B Occ A:Br128 b:32.1 occ:0.50 BRAC A:LJ3128 0.0 32.1 0.5 CAM A:LJ3128 2.0 25.3 0.5 CAJ A:LJ3128 2.9 25.6 0.5 OAA A:LJ3128 3.0 24.1 0.5 CAK A:LJ3128 3.0 25.7 0.5 O A:HOH194 3.5 23.5 1.0 CB A:ALA108 3.9 12.3 1.0 CD A:LYS15 4.0 17.3 1.0 CAL A:LJ3128 4.2 25.3 0.5 CAO A:LJ3128 4.2 24.0 0.5 CG2 A:THR106 4.3 15.5 1.0 CAI A:LJ3128 4.7 25.8 0.5 CE A:LYS15 4.7 23.2 1.0 O A:HOH160 4.8 31.3 1.0 CG A:LYS15 4.9 15.2 1.0 CG2 A:VAL121 4.9 19.3 1.0 CB A:LYS15 4.9 13.1 1.0

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


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 3,5-Dibromo-4- Hydroxybiphenyl within 5.0Å range: probe atom residue distance (Å) B Occ B:Br128 b:31.8 occ:0.50 BRAB B:LJ3128 0.0 31.8 0.5 CAL B:LJ3128 1.9 25.7 0.5 CAK B:LJ3128 2.8 24.4 0.5 CAI B:LJ3128 2.9 25.8 0.5 OAA B:LJ3128 3.0 23.0 0.5 CD1 B:LEU17 3.7 16.9 1.0 NZ B:LYS15 4.0 25.1 1.0 CAM B:LJ3128 4.2 24.6 0.5 CAO B:LJ3128 4.2 24.4 0.5 CE B:LYS15 4.5 21.9 1.0 CAJ B:LJ3128 4.7 25.0 0.5 CG B:LEU17 4.9 14.2 1.0 CD2 B:LEU17 4.9 16.2 1.0

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


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 3,5-Dibromo-4- Hydroxybiphenyl within 5.0Å range: probe atom residue distance (Å) B Occ B:Br128 b:31.3 occ:0.50 BRAC B:LJ3128 0.0 31.3 0.5 CAM B:LJ3128 1.9 24.6 0.5 CAK B:LJ3128 2.9 24.4 0.5 CAJ B:LJ3128 2.9 25.0 0.5 OAA B:LJ3128 3.1 23.0 0.5 O B:HOH194 3.5 23.5 1.0 CB B:ALA108 3.9 14.2 1.0 CD B:LYS15 4.1 18.8 1.0 CG2 B:THR106 4.1 16.7 1.0 CAL B:LJ3128 4.2 25.7 0.5 CAO B:LJ3128 4.2 24.4 0.5 CG2 B:VAL121 4.4 19.6 1.0 CAI B:LJ3128 4.7 25.8 0.5 NZ B:LYS15 4.7 25.1 1.0 O B:HOH180 4.8 33.9 1.0 CE B:LYS15 4.9 21.9 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