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Chlorine in PDB 6v90: Crystal Structure of the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12

Enzymatic activity of Crystal Structure of the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12

All present enzymatic activity of Crystal Structure of the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12, PDB code: 6v90 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) 44.47 / 2.04
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 45.360, 104.639, 168.863, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12 (pdb code 6v90). 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 the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12, PDB code: 6v90:

Chlorine binding site 1 out of 1 in 6v90

Go back to Chlorine Binding Sites List in 6v90
Chlorine binding site 1 out of 1 in the Crystal Structure of the P300 Acetyltransferase Domain with Accoa Competitive Inhibitor 12


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 Accoa Competitive Inhibitor 12 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1704

b:38.8
occ:1.00
 O A:HOH1849 3.0 31.7 1.0
O A:HOH1853 3.1 35.6 1.0
N A:LEU1398 3.3 33.5 1.0
CE2 A:TYR1446 3.7 37.4 1.0
CBD A:QSD1701 3.8 37.0 1.0
CA A:TYR1397 3.9 38.3 1.0
CG A:LEU1398 3.9 37.1 1.0
CD2 A:TYR1446 4.0 40.7 1.0
O A:LEU1398 4.0 35.1 1.0
C A:TYR1397 4.0 34.2 1.0
CD1 A:LEU1398 4.2 40.4 1.0
OH A:TYR1467 4.2 36.2 1.0
CA A:LEU1398 4.3 35.3 1.0
O A:CYS1438 4.4 41.0 1.0
O A:SER1396 4.5 36.8 1.0
CBC A:QSD1701 4.5 39.7 1.0
CB A:LEU1398 4.6 38.2 1.0
O A:TRP1436 4.6 30.9 1.0
C A:LEU1398 4.6 35.6 1.0
O A:HOH1845 4.6 33.1 1.0
N A:TYR1397 4.7 37.6 1.0
CBE A:QSD1701 4.8 39.3 1.0
CZ A:TYR1446 4.8 39.1 1.0
CB A:TYR1397 4.9 41.3 1.0
C A:SER1396 4.9 37.0 1.0
CD2 A:LEU1398 5.0 38.4 1.0

Reference:

J.E.Wilson, A.Huhn, A.S.Gardberg, F.Poy, F.Brucelle, V.Vivat, G.Patel, C.Patel, R.Cummings, R.Sims, J.Levell, J.E.Audia, A.Bommi-Reddy, N.Cantone. Early Drug Discovery Efforts Towards the Identification of EP300/Cbp Histone Acetyltransferase (Hat) Inhibitors. Chemmedchem 2020.
ISSN: ESSN 1860-7187
PubMed: 32181984
DOI: 10.1002/CMDC.202000007
Page generated: Sat Jul 12 20:48:30 2025

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