Chlorine in PDB 6pf1: Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa

All present enzymatic activity of Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa:
2.3.1.48;

The structure of Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa, PDB code: 6pf1 was solved by A.S.Gardberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.69 / 2.32
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.062, 90.634, 112.950, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 24.7

The structure of Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Chlorine atom in the Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa (pdb code 6pf1). 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 the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa, PDB code: 6pf1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa


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 the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1702 b:36.5 occ:1.00 CL1 A:OJ71702 0.0 36.5 1.0 C14 A:OJ71702 1.7 34.2 1.0 C13 A:OJ71702 2.7 33.6 1.0 C10 A:OJ71702 2.7 32.5 1.0 C3 A:OJ71702 3.1 28.0 1.0 C1 A:OJ71702 3.4 29.3 1.0 C2 A:OJ71702 3.4 27.4 1.0 CE2 A:TRP1509 3.5 34.5 1.0 NE1 A:TRP1509 3.6 34.8 1.0 CG2 A:ILE1486 3.7 32.8 1.0 CD2 A:TRP1509 3.8 32.8 1.0 CD1 A:ILE1486 3.8 34.4 1.0 CD2 A:LEU1501 3.9 36.1 1.0 CD1 A:TRP1509 3.9 33.5 1.0 CZ2 A:TRP1509 4.0 32.7 1.0 CB A:ILE1486 4.0 32.8 1.0 C12 A:OJ71702 4.0 38.6 1.0 N2 A:OJ71702 4.0 33.4 1.0 CG A:TRP1509 4.0 31.6 1.0 SD A:MET1588 4.0 44.4 1.0 C4 A:OJ71702 4.2 25.3 1.0 CG A:MET1588 4.3 44.4 1.0 N1 A:OJ71702 4.4 27.9 1.0 C11 A:OJ71702 4.5 34.5 1.0 CE3 A:TRP1509 4.5 32.9 1.0 CG1 A:ILE1486 4.5 33.6 1.0 CD1 A:LEU1501 4.5 36.8 1.0 CH2 A:TRP1509 4.5 33.8 1.0 CZ3 A:TRP1509 4.8 33.2 1.0 CG A:LEU1501 4.8 35.8 1.0 C5 A:OJ71702 4.9 25.8 1.0 CB A:TRP1509 4.9 30.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa


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 the P300 Acetyltransferase Domain with Allosteric Inhibitor Cpi-090 and Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1702 b:42.1 occ:1.00 CL1 B:OJ71702 0.0 42.1 1.0 C14 B:OJ71702 1.7 38.5 1.0 C13 B:OJ71702 2.7 38.1 1.0 C10 B:OJ71702 2.7 34.9 1.0 C3 B:OJ71702 3.1 31.1 1.0 C1 B:OJ71702 3.2 31.1 1.0 C2 B:OJ71702 3.3 31.1 1.0 CE2 B:TRP1509 3.6 43.0 1.0 NE1 B:TRP1509 3.8 43.0 1.0 CG2 B:ILE1486 3.8 32.2 1.0 CD1 B:ILE1486 3.8 36.0 1.0 CD2 B:TRP1509 3.8 41.2 1.0 N2 B:OJ71702 4.0 36.4 1.0 C12 B:OJ71702 4.0 39.6 1.0 CZ2 B:TRP1509 4.0 42.2 1.0 CD1 B:TRP1509 4.1 40.8 1.0 CG B:TRP1509 4.1 41.3 1.0 CB B:ILE1486 4.1 33.2 1.0 SD B:MET1588 4.2 50.4 1.0 C4 B:OJ71702 4.2 30.1 1.0 CD2 B:LEU1501 4.4 41.4 1.0 CE3 B:TRP1509 4.4 39.6 1.0 N1 B:OJ71702 4.4 30.5 1.0 C11 B:OJ71702 4.4 34.8 1.0 CH2 B:TRP1509 4.5 39.1 1.0 CG B:MET1588 4.5 46.6 1.0 CG1 B:ILE1486 4.6 36.1 1.0 CZ3 B:TRP1509 4.7 37.8 1.0 CD1 B:LEU1501 4.7 45.0 1.0 C5 B:OJ71702 4.9 28.3 1.0 CG B:LEU1501 4.9 42.3 1.0

A.S.Gardberg, A.J.Huhn, R.Cummings, A.Bommi-Reddy, F.Poy, J.Setser, V.Vivat, F.Brucelle, J.Wilson. Make the Right Measurement: Discovery of An Allosteric Inhibition Site For P300-Hat. Struct Dyn. V. 6 54702 2019.
ISSN: ESSN 2329-7778
PubMed: 31649965
DOI: 10.1063/1.5119336