Chlorine in PDB 6bn7: Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac.

The structure of Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac., PDB code: 6bn7 was solved by R.P.Nowak, S.L.Deangelo, D.Buckley, J.E.Bradner, E.S.Fischer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.87 / 3.50
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	115.571, 115.571, 596.315, 90.00, 90.00, 120.00
R / Rfree (%)	21.2 / 25.6

The structure of Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac. (pdb code 6bn7). 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 DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac., PDB code: 6bn7:

Chlorine binding site 1 out of 1 in the Crystal Structure of DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac.


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 DDB1-Crbn-BRD4(BD1) Complex Bound to DBET23 Protac. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:0.6 occ:1.00 CL B:RN3502 0.0 0.6 1.0 C11 B:RN3502 1.7 0.8 1.0 C10 B:RN3502 2.7 1.0 1.0 C12 B:RN3502 2.7 1.0 1.0 CD2 B:HIS353 3.3 0.2 1.0 C9 B:RN3502 4.0 0.1 1.0 C13 B:RN3502 4.0 0.8 1.0 NE2 B:HIS353 4.1 0.3 1.0 CG B:HIS353 4.1 0.2 1.0 CB C:ASP145 4.2 0.4 1.0 SD C:MET149 4.5 0.5 1.0 CB B:HIS353 4.5 0.2 1.0 C8 B:RN3502 4.5 0.1 1.0 OD2 C:ASP145 4.6 0.9 1.0 CZ2 C:TRP81 4.7 0.5 1.0 CH2 C:TRP81 4.9 0.1 1.0 CG C:ASP145 4.9 0.0 1.0

R.P.Nowak, S.L.Deangelo, D.Buckley, Z.He, K.A.Donovan, J.An, N.Safaee, M.P.Jedrychowski, C.M.Ponthier, M.Ishoey, T.Zhang, J.D.Mancias, N.S.Gray, J.E.Bradner, E.S.Fischer. Plasticity in Binding Confers Selectivity in Ligand-Induced Protein Degradation. Nat. Chem. Biol. V. 14 706 2018.
ISSN: ESSN 1552-4469
PubMed: 29892083
DOI: 10.1038/S41589-018-0055-Y