Potassium in PDB 4a9k: Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide

All present enzymatic activity of Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide:
2.3.1.48;

The structure of Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide, PDB code: 4a9k was solved by C.W.Chung, P.Bamborough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.47 / 1.81
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	120.943, 120.943, 40.471, 90.00, 90.00, 120.00
R / Rfree (%)	16 / 19.7

The binding sites of Potassium atom in the Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide (pdb code 4a9k). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide, PDB code: 4a9k:

Potassium binding site 1 out of 1 in the Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Bromodomain of Human Crebbp with N-(4-Hydroxyphenyl)Acetamide within 5.0Å range: probe atom residue distance (Å) B Occ B:K2197 b:35.2 occ:1.00 O B:HOH2011 2.7 44.7 1.0 O B:TRP1165 2.8 27.9 1.0 O B:ASN1168 2.8 30.9 1.0 O B:HOH2012 2.8 42.5 1.0 O B:LEU1166 3.0 28.9 1.0 O B:HOH2098 3.0 48.4 1.0 C B:LEU1166 3.7 28.3 1.0 C B:ASN1168 3.8 30.8 1.0 C B:TRP1165 3.9 27.4 1.0 CA B:LEU1166 4.1 28.2 1.0 O B:HOH2096 4.3 31.1 1.0 CA B:ARG1169 4.4 34.5 1.0 N B:ASN1168 4.5 28.3 1.0 N B:LEU1166 4.5 26.9 1.0 N B:ARG1169 4.5 33.0 1.0 CE2 B:TYR1175 4.5 29.5 1.0 C B:TYR1167 4.6 28.7 1.0 N B:TYR1167 4.7 27.5 1.0 CD2 B:TYR1175 4.7 28.2 1.0 CA B:ASN1168 4.8 29.6 1.0 O B:TYR1167 4.8 28.7 1.0 N B:LYS1170 4.9 34.7 1.0 C B:ARG1169 4.9 33.7 1.0

C.W.Chung, A.W.Dean, J.M.Woolven, P.Bamborough. Fragment-Based Discovery of Bromodomain Inhibitors Part 1: Inhibitor Binding Modes and Implications For Lead Discovery. J.Med.Chem. V. 55 576 2012.
ISSN: ISSN 0022-2623
PubMed: 22136404
DOI: 10.1021/JM201320W