Chlorine in PDB 4tt6: Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form

All present enzymatic activity of Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form:
3.6.1.3;

The structure of Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form, PDB code: 4tt6 was solved by G.Poncet-Montange, Y.Zhan, J.Bardenhagen, A.Petrocchi, E.Leo, X.Shi, G.Lee, P.Leonard, M.Geck Do, M.Cardozo, W.Palmer, J.Andersen, P.Jones, J.Ladbury, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.83 / 2.00
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	79.639, 79.639, 138.271, 90.00, 90.00, 120.00
R / Rfree (%)	16.5 / 17.7

The binding sites of Chlorine atom in the Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form (pdb code 4tt6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form, PDB code: 4tt6:

Chlorine binding site 1 out of 1 in the Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of ATAD2A Bromodomain Double Mutant N1063A-Y1064A in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1202 b:70.3 occ:1.00 NH2 A:ARG1077 3.4 28.9 1.0 NH1 A:ARG1077 3.5 26.5 1.0 O A:HOH1403 3.9 42.3 1.0 CZ A:ARG1077 3.9 24.5 1.0 CD2 A:LEU1073 4.5 30.5 1.0 O A:HOH1406 4.8 42.6 1.0

G.Poncet-Montange, Y.Zhan, J.P.Bardenhagen, A.Petrocchi, E.Leo, X.Shi, G.R.Lee Iv, P.G.Leonard, M.K.Geck Do, M.G.Cardozo, J.N.Andersen, W.S.Palmer, P.Jones, J.E.Ladbury. Observed Bromodomain Flexibility Reveals Histone Peptide- and Small Molecule Ligand-Compatible Forms of ATAD2A. Biochem.J. 2014.
ISSN: ESSN 1470-8728
PubMed: 25486442
DOI: 10.1042/BJ20140933