Bromine in PDB 4by7: Elongating Rna Polymerase II-BYE1 Tld Complex

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

The structure of Elongating Rna Polymerase II-BYE1 Tld Complex, PDB code: 4by7 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)	48.84 / 3.15
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	222.500, 390.680, 281.970, 90.00, 90.00, 90.00
R / Rfree (%)	18.94 / 21.19

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

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

The binding sites of Bromine atom in the Elongating Rna Polymerase II-BYE1 Tld Complex (pdb code 4by7). 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 Elongating Rna Polymerase II-BYE1 Tld Complex, PDB code: 4by7:

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


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Elongating Rna Polymerase II-BYE1 Tld Complex within 5.0Å range: probe atom residue distance (Å) B Occ T:Br19 b:0.2 occ:1.00 BR T:BRU19 0.0 0.2 1.0 C5 T:BRU19 1.9 0.3 1.0 C6 T:BRU19 2.9 0.6 1.0 C4 T:BRU19 3.0 0.6 1.0 O4 T:BRU19 3.2 0.3 1.0 C5 T:DC18 3.6 98.9 1.0 C6 T:DC18 3.7 99.5 1.0 C4 T:DC18 3.7 97.9 1.0 OP1 T:BRU19 3.8 98.3 1.0 N3 T:DC18 3.9 97.2 1.0 N1 T:DC18 3.9 98.8 1.0 C2 T:DC18 4.0 97.7 1.0 N1 T:BRU19 4.1 97.0 1.0 N3 T:BRU19 4.2 98.3 1.0 N4 T:DC18 4.3 97.6 1.0 C3' T:DC18 4.3 0.5 1.0 C2' T:DC18 4.4 99.1 1.0 O5' T:BRU19 4.6 97.5 1.0 C2 T:BRU19 4.7 95.3 1.0 C1' T:DC18 4.7 99.6 1.0 O2 T:DC18 4.8 97.1 1.0 P T:BRU19 4.8 98.9 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