Chlorine in PDB 3drg: Lactococcal Oppa Complexed with Bradykinin in the Closed Conformation

The structure of Lactococcal Oppa Complexed with Bradykinin in the Closed Conformation, PDB code: 3drg was solved by R.P.-A.Berntsson, M.K.Doeven, R.H.Duurkens, D.Sengupta, S.-J.Marrink, A.-M.Thunnissen, B.Poolman, D.-J.Slotboom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.32 / 2.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	42.175, 58.636, 61.277, 100.97, 101.12, 103.02
R / Rfree (%)	21.8 / 27.5

The binding sites of Chlorine atom in the Lactococcal Oppa Complexed with Bradykinin in the Closed Conformation (pdb code 3drg). 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 Lactococcal Oppa Complexed with Bradykinin in the Closed Conformation, PDB code: 3drg:

Chlorine binding site 1 out of 1 in the Lactococcal Oppa Complexed with Bradykinin in the Closed Conformation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Lactococcal Oppa Complexed with Bradykinin in the Closed Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:43.9 occ:1.00 O A:HOH807 3.3 26.0 1.0 N A:GLY145 3.4 32.3 1.0 CA A:GLY145 3.7 32.5 1.0 NZ A:LYS176 3.8 34.4 1.0 OD2 A:ASP148 3.8 34.6 1.0 CG A:ASP148 3.9 34.3 1.0 CE A:LYS176 4.1 34.4 1.0 CB A:SER147 4.2 33.7 1.0 N A:ASP148 4.2 34.1 1.0 C A:GLY145 4.3 32.6 1.0 OD1 A:ASP148 4.3 34.3 1.0 CB A:ASP148 4.5 34.3 1.0 N A:SER147 4.5 33.4 1.0 N A:LEU146 4.5 32.7 1.0 C A:VAL144 4.6 32.2 1.0 CA A:SER147 4.7 33.7 1.0 OG A:SER147 4.9 34.0 1.0 C A:SER147 4.9 33.9 1.0 CA A:ASP148 4.9 34.3 1.0 O A:GLY145 5.0 32.6 1.0 CA A:VAL144 5.0 32.1 1.0

R.P.-A.Berntsson, M.K.Doeven, F.Fusetti, R.H.Duurkens, D.Sengupta, S.-J.Marrink, A.-M.Thunnissen, B.Poolman, D.-J.Slotboom. The Structural Basis For Peptide Selection By the Transport Receptor Oppa Embo J. V. 28 1332 2009.
ISSN: ISSN 0261-4189
PubMed: 19300437
DOI: 10.1038/EMBOJ.2009.65