Chlorine in PDB 6siq: Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface

The structure of Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface, PDB code: 6siq was solved by S.Leysen, M.Wolter, X.Guillory, S.Genet, B.Somsen, J.Patel, P.Castaldi, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.59 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.340, 112.004, 62.572, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 21.8

The binding sites of Chlorine atom in the Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface (pdb code 6siq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface, PDB code: 6siq:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:17.0 occ:1.00 O A:HOH685 3.0 23.6 1.0 O A:HOH633 3.0 18.6 1.0 CA A:TYR84 3.8 8.8 1.0 O A:GLU83 3.9 10.3 1.0 CD A:LYS87 3.9 23.8 1.0 N A:TYR84 4.0 7.5 1.0 C A:GLU83 4.0 8.9 1.0 CB A:LYS87 4.1 10.9 1.0 CD1 A:TYR84 4.1 6.5 1.0 CB A:TYR84 4.2 9.5 1.0 CB A:GLU83 4.4 8.1 1.0 O A:HOH725 4.4 40.1 1.0 O A:HOH446 4.5 17.8 1.0 CG A:LYS87 4.6 16.4 1.0 CG A:TYR84 4.6 6.3 1.0 O A:HOH688 4.8 40.3 1.0 CA A:GLU83 4.9 9.7 1.0

Chlorine binding site 2 out of 3 in the Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:36.2 occ:1.00 CL A:LF5302 0.0 36.2 1.0 C08 A:LF5302 1.8 35.3 1.0 C07 A:LF5302 2.7 30.7 1.0 H071 A:LF5302 2.8 36.7 1.0 C09 A:LF5302 2.8 40.2 1.0 H131 A:LF5302 2.9 39.8 1.0 C13 A:LF5302 3.2 33.3 1.0 OD1 A:ASN42 3.3 17.8 0.7 O A:HOH496 3.8 26.4 1.0 C06 A:LF5302 4.0 35.4 1.0 CG A:ASN42 4.0 12.6 0.7 ND2 A:ASN42 4.0 7.2 0.3 C10 A:LF5302 4.0 30.9 1.0 O P:HOH421 4.1 38.6 1.0 CG A:ASN42 4.2 11.8 0.3 OD1 A:ASN42 4.4 20.5 0.3 C05 A:LF5302 4.5 30.4 1.0 O A:HOH703 4.5 28.7 1.0 C12 A:LF5302 4.6 24.0 1.0 O P:HOH408 4.7 38.7 1.0 H061 A:LF5302 4.7 42.4 1.0 O A:HOH434 4.7 25.9 1.0 CB A:ASN42 4.7 8.7 0.3 CB A:ASN42 4.7 8.4 0.7 ND2 A:ASN42 4.8 13.3 0.7

Chlorine binding site 3 out of 3 in the Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Fragment Az-012 Binding at the P53PT387/14-3-3 Sigma Interface within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:36.0 occ:1.00 CL A:LF5303 0.0 36.0 1.0 C08 A:LF5303 1.8 32.1 1.0 C07 A:LF5303 2.7 34.1 1.0 C09 A:LF5303 2.8 32.5 1.0 H071 A:LF5303 2.8 40.9 1.0 H131 A:LF5303 2.9 37.7 1.0 C13 A:LF5303 3.2 31.5 1.0 O A:GLN93 3.2 10.9 1.0 CD2 A:LEU131 3.5 10.6 1.0 CB A:GLN93 3.8 10.3 1.0 CB A:ASP97 3.9 10.4 1.0 C A:GLN93 3.9 12.7 1.0 CD1 A:LEU131 4.0 11.1 1.0 C06 A:LF5303 4.0 33.3 1.0 C10 A:LF5303 4.0 42.6 1.0 CA A:GLN93 4.1 8.4 1.0 N A:ASP97 4.3 8.5 1.0 CG A:LEU131 4.4 9.1 1.0 CG A:GLN93 4.4 10.3 1.0 CA A:ASP97 4.5 8.1 1.0 C12 A:LF5303 4.5 28.8 1.0 C05 A:LF5303 4.6 42.3 1.0 CG A:ASP97 4.7 23.6 1.0 OD1 A:ASP97 4.7 25.3 1.0 H061 A:LF5303 4.8 39.9 1.0 N A:GLY94 5.0 12.0 1.0 H1 A:LF5303 5.0 49.2 1.0

X.Guillory, M.Wolter, S.Leysen, J.F.Neves, A.Kuusk, S.Genet, B.Somsen, J.Morrow, E.Rivers, L.Van Beek, J.Patel, R.Goodnow, H.Schoenherr, N.Fuller, Q.Cao, R.G.Doveston, L.Brunsveld, M.R.Arkin, M.P.Castaldi, H.Boyd, I.Landrieu, H.Chen, C.Ottmann. Fragment-Based Differential Targeting of Ppi Stabilizer Interfaces. J.Med.Chem. 2020.
ISSN: ISSN 0022-2623
PubMed: 32501690
DOI: 10.1021/ACS.JMEDCHEM.9B01942