Chlorine in PDB 6fkc: Crystal Structure of N2C/D282C Stabilized Opsin Bound to RS15

The structure of Crystal Structure of N2C/D282C Stabilized Opsin Bound to RS15, PDB code: 6fkc was solved by D.Mattle, J.Standfuss, R.Dawson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.40 / 2.46
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	243.214, 243.214, 111.858, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 24

The binding sites of Chlorine atom in the Crystal Structure of N2C/D282C Stabilized Opsin Bound to RS15 (pdb code 6fkc). 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 N2C/D282C Stabilized Opsin Bound to RS15, PDB code: 6fkc:

Chlorine binding site 1 out of 1 in the Crystal Structure of N2C/D282C Stabilized Opsin Bound to RS15


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 N2C/D282C Stabilized Opsin Bound to RS15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:83.4 occ:1.00 CL A:DLB407 0.0 83.4 1.0 C13 A:DLB407 1.7 80.7 1.0 C14 A:DLB407 2.7 77.4 1.0 C12 A:DLB407 2.7 69.6 1.0 CD1 A:TRP265 3.8 66.8 1.0 CA A:TRP265 3.8 64.3 1.0 O A:CYS264 3.9 89.3 1.0 C15 A:DLB407 4.0 71.6 1.0 C11 A:DLB407 4.0 69.5 1.0 CB A:TRP265 4.0 58.0 1.0 SG A:CYS264 4.1 83.3 1.0 C A:CYS264 4.1 73.4 1.0 N A:TRP265 4.2 68.5 1.0 CG A:TRP265 4.2 64.5 1.0 CE1 A:PHE212 4.2 67.6 1.0 C7' A:BOG409 4.3 83.2 1.0 CD1 A:PHE212 4.4 70.8 1.0 C10 A:DLB407 4.5 74.9 1.0 CZ A:PHE261 4.5 69.5 1.0 CE1 A:PHE261 4.6 69.0 1.0 C8' A:BOG409 4.6 86.6 1.0 CD1 A:LEU125 4.7 54.4 1.0 CB A:CYS264 4.7 69.3 1.0 CD1 A:TYR268 4.7 73.7 1.0 NE1 A:TRP265 4.9 70.0 1.0

D.Mattle, B.Kuhn, J.Aebi, M.Bedoucha, D.Kekilli, N.Grozinger, A.Alker, M.G.Rudolph, G.Schmid, G.F.X.Schertler, M.Hennig, J.Standfuss, R.J.P.Dawson. Ligand Channel in Pharmacologically Stabilized Rhodopsin. Proc. Natl. Acad. Sci. V. 115 3640 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29555765
DOI: 10.1073/PNAS.1718084115