Chlorine in PDB 4tt4: Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide

All present enzymatic activity of Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide:
3.6.1.3;

The structure of Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide, PDB code: 4tt4 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)	79.01 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	108.160, 115.680, 77.500, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 24

The binding sites of Chlorine atom in the Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide (pdb code 4tt4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide, PDB code: 4tt4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide


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 Complexed with H3(1-21)K14AC Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1203 b:65.5 occ:1.00 NH2 A:ARG1075 3.3 62.3 1.0 NE A:ARG1072 3.8 74.9 1.0 NH2 A:ARG1072 4.3 82.3 1.0 CZ A:ARG1072 4.5 79.2 1.0 CZ A:ARG1075 4.5 59.2 1.0 CD A:ARG1072 4.6 67.4 1.0 NE A:ARG1075 4.9 56.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of ATAD2A Bromodomain Complexed with H3(1-21)K14AC Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1203 b:66.1 occ:1.00 NH2 B:ARG1075 3.1 60.9 1.0 NE2 A:GLN981 3.8 71.3 1.0 CD B:ARG1072 3.9 74.4 1.0 NE B:ARG1072 4.0 82.4 1.0 CZ B:ARG1075 4.0 59.2 1.0 CG A:GLN981 4.1 59.0 1.0 NE B:ARG1075 4.1 55.5 1.0 CD A:GLN981 4.3 65.1 1.0 NE2 B:HIS1076 4.4 69.8 1.0 CD2 B:HIS1076 4.5 64.5 1.0 CB A:GLN981 4.5 53.4 1.0 CG B:ARG1072 4.7 68.9 1.0 O A:HOH1322 4.8 38.3 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