Bromine in PDB 4bxx: Arrested Rna Polymerase II-BYE1 Complex

All present enzymatic activity of Arrested Rna Polymerase II-BYE1 Complex:
2.7.7.6;

The structure of Arrested Rna Polymerase II-BYE1 Complex, PDB code: 4bxx was solved by K.Kinkelin, G.G.Wozniak, S.B.Rothbart, M.Lidschreiber, B.D.Strahl, P.Cramer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.08 / 3.28
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	222.920, 392.670, 281.040, 90.00, 90.00, 90.00
R / Rfree (%)	17.98 / 20.77

The structure of Arrested Rna Polymerase II-BYE1 Complex also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Zinc	(Zn)	8 atoms

The binding sites of Bromine atom in the Arrested Rna Polymerase II-BYE1 Complex (pdb code 4bxx). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Arrested Rna Polymerase II-BYE1 Complex, PDB code: 4bxx:

Bromine binding site 1 out of 1 in the Arrested Rna Polymerase II-BYE1 Complex


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Arrested Rna Polymerase II-BYE1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ T:Br22 b:0.7 occ:1.00 BR T:BRU22 0.0 0.7 1.0 C5 T:BRU22 1.9 0.6 1.0 C6 T:BRU22 2.9 0.7 1.0 C4 T:BRU22 3.0 0.5 1.0 O4 T:BRU22 3.2 0.4 1.0 C4 T:DG21 3.6 0.5 1.0 C5 T:DG21 3.7 0.4 1.0 N9 T:DG21 3.8 0.7 1.0 N7 T:DG21 3.9 0.9 1.0 C8 T:DG21 4.0 0.5 1.0 C2' T:DG21 4.0 0.8 1.0 OE2 B:GLU1120 4.1 0.3 1.0 N3 T:DG21 4.1 0.7 1.0 N1 T:BRU22 4.2 0.6 1.0 C6 T:DG21 4.2 0.9 1.0 N3 T:BRU22 4.2 0.1 1.0 CD B:GLU1120 4.4 0.3 1.0 OE1 B:GLU1120 4.4 0.1 1.0 C2 T:DG21 4.5 0.1 1.0 N1 T:DG21 4.5 0.9 1.0 C1' T:DG21 4.5 0.0 1.0 C2 T:BRU22 4.7 0.9 1.0 C3' T:DG21 4.7 0.9 1.0 O6 T:DG21 4.9 0.1 1.0 OP1 T:BRU22 4.9 0.2 1.0

K.Kinkelin, G.G.Wozniak, S.B.Rothbart, M.Lidschreiber, B.D.Strahl, P.Cramer. Structures of Rna Polymerase II Complexes with BYE1, A Chromatin-Binding PHF3/DIDO1 Homologue Proc.Natl.Acad.Sci.Usa V. 110 15277 2013.
ISSN: ISSN 0027-8424
PubMed: 24003114
DOI: 10.1073/PNAS.1311010110