Chlorine in PDB 3ixp: Crystal Structure of the Ecdysone Receptor Bound to BYI08346

The structure of Crystal Structure of the Ecdysone Receptor Bound to BYI08346, PDB code: 3ixp was solved by D.Moras, I.M.L.Billas, C.Browning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.85
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	147.875, 147.875, 59.776, 90.00, 90.00, 120.00
R / Rfree (%)	22.1 / 27.1

The binding sites of Chlorine atom in the Crystal Structure of the Ecdysone Receptor Bound to BYI08346 (pdb code 3ixp). 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 Ecdysone Receptor Bound to BYI08346, PDB code: 3ixp:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Ecdysone Receptor Bound to BYI08346


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 Ecdysone Receptor Bound to BYI08346 within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl800 b:47.4 occ:1.00 CL8 D:834800 0.0 47.4 1.0 C5 D:834800 1.7 51.6 1.0 C4 D:834800 2.7 53.0 1.0 C6 D:834800 2.8 52.8 1.0 C7 D:834800 3.2 51.7 1.0 N18 D:834800 3.3 51.0 1.0 OD1 D:ASN504 3.3 41.1 1.0 N12 D:834800 3.5 51.4 1.0 CE D:MET381 3.6 45.9 1.0 CG D:ASN504 3.7 41.9 1.0 C3 D:834800 4.0 54.5 1.0 CB D:MET380 4.1 47.2 1.0 C1 D:834800 4.1 54.7 1.0 CH2 D:TRP526 4.1 63.6 1.0 N9 D:834800 4.2 51.2 1.0 CB D:SER377 4.2 41.8 1.0 ND2 D:ASN504 4.2 40.9 1.0 CZ2 D:TRP526 4.2 63.5 1.0 CA D:SER377 4.3 41.8 1.0 C19 D:834800 4.4 49.4 1.0 O D:SER377 4.4 41.9 1.0 CB D:ASN504 4.5 41.8 1.0 CG D:MET380 4.5 52.2 1.0 C11 D:834800 4.6 51.4 1.0 C2 D:834800 4.6 54.4 1.0 C35 D:834800 4.6 46.9 1.0 C36 D:834800 4.8 46.2 1.0 SD D:MET381 4.8 42.3 1.0 C D:SER377 4.8 41.3 1.0 SD D:MET380 4.9 62.4 1.0 C10 D:834800 4.9 51.6 1.0

D.Moras, I.M.L.Billas, C.Browning. Adaptability of the Ecdysone Receptor Bound to Synthetic Ligands To Be Published.