Bromine in PDB 4fi8: Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide

The structure of Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide, PDB code: 4fi8 was solved by S.Connelly, N.Grimster, I.A.Wilson, J.W.Kelly, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	86.14 / 1.22
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	43.185, 86.143, 63.693, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19.7

The structure of Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Bromine atom in the Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide (pdb code 4fi8). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide, PDB code: 4fi8:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Br301 b:45.6 occ:0.50 BR1 A:0UC301 0.0 45.6 0.5 C16 A:0UC301 1.9 31.9 0.5 C17 A:0UC301 2.7 31.9 0.5 C15 A:0UC301 2.9 25.3 0.5 O11 A:0UC301 3.3 20.2 0.5 C12 A:0UC301 3.4 20.1 0.5 CB A:ALA108 3.8 16.1 1.0 C18 A:0UC301 4.0 29.5 0.5 CG2 A:VAL121 4.1 23.7 1.0 C20 A:0UC301 4.2 26.1 0.5 CG2 A:THR106 4.4 19.6 1.0 C10 A:0UC301 4.5 18.3 0.5 C19 A:0UC301 4.6 28.4 0.5 N13 A:0UC301 4.7 23.8 0.5 CG2 A:THR119 4.8 16.6 1.0 O A:HOH419 5.0 39.5 1.0

Bromine binding site 2 out of 2 in the Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Kinetic Stabilization of Transthyretin Through Covalent Modification of K15 By 4-Bromo-3-(5-(3,5-Dichloro-4-Hydroxyphenyl)-1,3,4- Oxadiazol-2-Yl)-Benzenesulfonamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Br301 b:46.0 occ:0.50 BR1 B:0UC301 0.0 46.0 0.5 C16 B:0UC301 1.9 30.7 0.5 C17 B:0UC301 2.8 29.5 0.5 C15 B:0UC301 2.9 27.3 0.5 O11 B:0UC301 3.1 21.0 0.5 C12 B:0UC301 3.3 23.1 0.5 CG2 B:VAL121 3.6 22.8 1.0 CB B:ALA108 3.8 16.8 1.0 C18 B:0UC301 4.1 30.1 0.5 C20 B:0UC301 4.1 28.1 0.5 C10 B:0UC301 4.4 19.9 0.5 N13 B:0UC301 4.5 24.1 0.5 CG2 B:THR106 4.5 22.1 1.0 C19 B:0UC301 4.6 31.0 0.5 CB B:VAL121 4.8 19.0 1.0 CD B:LYS15 4.9 22.6 0.5 CG2 B:THR119 4.9 16.5 1.0

N.P.Grimster, S.Connelly, A.Baranczak, J.Dong, L.B.Krasnova, K.B.Sharpless, E.T.Powers, I.A.Wilson, J.W.Kelly. Aromatic Sulfonyl Fluorides Covalently Kinetically Stabilize Transthyretin to Prevent Amyloidogenesis While Affording A Fluorescent Conjugate. J.Am.Chem.Soc. V. 135 5656 2013.
ISSN: ISSN 0002-7863
PubMed: 23350654
DOI: 10.1021/JA311729D