Chlorine in PDB 9em5: OPR3 Variant Y364P in Its Monomeric Form

All present enzymatic activity of OPR3 Variant Y364P in Its Monomeric Form:
1.3.1.42;

The structure of OPR3 Variant Y364P in Its Monomeric Form, PDB code: 9em5 was solved by A.Bijelic, P.Macheroux, B.Kerschbaumer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.39 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.338, 89.941, 51.284, 90, 105.63, 90
R / Rfree (%)	18.4 / 20.8

The binding sites of Chlorine atom in the OPR3 Variant Y364P in Its Monomeric Form (pdb code 9em5). 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 OPR3 Variant Y364P in Its Monomeric Form, PDB code: 9em5:

Chlorine binding site 1 out of 1 in the OPR3 Variant Y364P in Its Monomeric Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of OPR3 Variant Y364P in Its Monomeric Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:26.3 occ:1.00 O2 A:MPD402 2.9 32.9 1.0 ND1 A:HIS188 3.0 20.6 1.0 NE2 A:HIS185 3.1 18.3 1.0 C2 A:FMN401 3.4 16.6 1.0 CE2 A:TYR190 3.4 19.4 1.0 N1 A:FMN401 3.5 15.0 1.0 N3 A:FMN401 3.5 14.9 1.0 C4 A:FMN401 3.5 14.2 1.0 C10 A:FMN401 3.6 16.4 1.0 C4A A:FMN401 3.6 14.4 1.0 C2 A:MPD402 3.7 33.8 1.0 C1 A:MPD402 3.8 26.7 1.0 O4 A:MPD402 3.8 38.3 1.0 C3 A:MPD402 3.8 32.8 1.0 CE1 A:HIS185 3.9 16.9 1.0 CG A:HIS188 3.9 17.7 1.0 O2 A:FMN401 3.9 16.1 1.0 CE1 A:HIS188 3.9 23.7 1.0 CB A:HIS188 4.0 18.0 1.0 CD2 A:TYR190 4.1 17.3 1.0 CD2 A:HIS185 4.2 19.4 1.0 O4 A:FMN401 4.3 14.5 1.0 OH A:TYR190 4.4 22.2 1.0 CZ A:TYR190 4.4 20.3 1.0 N10 A:FMN401 4.4 16.8 1.0 N5 A:FMN401 4.4 15.5 1.0 C4 A:MPD402 4.5 36.5 1.0 CZ2 A:TRP108 4.8 17.6 1.0

B.Kerschbaumer, P.Macheroux, A.Bijelic. Analysis of Homodimer Formation in 12-Oxophytodienoate Reductase 3 in Solutio and Crystallo Challenges the Physiological Role of the Dimer Sci Rep 2024.
ISSN: ESSN 2045-2322
DOI: 10.1038/S41598-024-69160-6