Chlorine in PDB 3t8o: Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution

All present enzymatic activity of Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution:
2.7.11.14;

The structure of Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution, PDB code: 3t8o was solved by J.J.G.Tesmer, P.Singh, M.R.Nance, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.60 / 2.50
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	55.541, 149.808, 190.879, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 24.5

The structure of Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution (pdb code 3t8o). 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 Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution, PDB code: 3t8o:

Chlorine binding site 1 out of 1 in the Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Rhodopsin Kinase (GRK1) L166K Mutant at 2.5A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl565 b:67.8 occ:1.00 NH1 A:ARG290 3.3 57.5 1.0 CD A:ARG290 3.5 50.4 1.0 N A:GLN287 3.6 52.2 1.0 NE2 A:GLN287 3.7 64.9 1.0 CA A:PHE286 4.1 49.9 1.0 CB A:GLN287 4.2 55.0 1.0 CZ A:ARG290 4.3 54.0 1.0 CD2 A:PHE286 4.3 48.3 1.0 NE A:ARG290 4.3 51.7 1.0 C A:PHE286 4.4 51.1 1.0 CB A:PHE286 4.4 47.5 1.0 CG A:GLN287 4.5 59.9 1.0 CA A:GLN287 4.5 53.1 1.0 CB A:ARG290 4.6 47.3 1.0 CD A:GLN287 4.6 63.7 1.0 CG A:ARG290 4.6 47.9 1.0 CG A:PHE286 4.7 46.1 1.0 O A:GLY285 4.7 53.2 1.0

J.J.Tesmer, M.R.Nance, P.Singh, H.Lee. Structure of A Monomeric Variant of Rhodopsin Kinase at 2.5 A Resolution. Acta Crystallogr.,Sect.F V. 68 622 2012.
ISSN: ESSN 1744-3091
PubMed: 22684056
DOI: 10.1107/S1744309112017435