Chlorine in PDB 5cyv: Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa

The structure of Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa, PDB code: 5cyv was solved by P.J.Stogios, X.Xu, A.Dong, A.Savchenko, A.Joachimiak, Midwest Center Forstructural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.79 / 1.52
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	64.145, 134.385, 73.336, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 20.2

The structure of Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa (pdb code 5cyv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa, PDB code: 5cyv:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa


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 Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl205 b:37.4 occ:0.84 O A:HOH451 3.1 29.4 1.0 O B:HOH347 3.2 28.1 1.0 CZ A:ARG38 3.5 21.0 1.0 O B:HOH346 3.7 38.1 1.0 NE A:ARG38 3.7 18.2 1.0 NH2 A:ARG38 3.7 20.4 1.0 NH1 A:ARG38 3.8 21.4 1.0 O B:HOH437 3.9 39.6 1.0 C8 B:WCA201 3.9 19.0 1.0 C2' B:WCA201 4.1 18.1 1.0 O2' B:WCA201 4.1 21.7 1.0 CD A:ARG38 4.2 17.6 1.0 O A:HOH494 4.2 43.1 1.0 O B:HOH427 4.3 37.9 1.0 O A:HOH399 4.6 34.5 1.0 O B:HOH353 4.7 20.6 1.0 N7 B:WCA201 4.8 18.4 1.0 O A:HOH409 4.9 23.2 1.0 O A:HOH499 4.9 43.9 1.0 N9 B:WCA201 4.9 19.2 1.0 OAK B:WCA201 4.9 21.9 1.0 CL A:CL206 5.0 32.5 0.7

Chlorine binding site 2 out of 3 in the Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl206 b:32.5 occ:0.65 O A:HOH494 2.9 43.1 1.0 O A:HOH342 3.0 29.6 1.0 NH2 A:ARG38 3.0 20.4 1.0 O A:HOH354 3.2 48.6 1.0 CD A:ARG38 3.4 17.6 1.0 CZ A:ARG38 4.0 21.0 1.0 CB A:GLN68 4.1 24.4 1.0 CD1 A:LEU72 4.2 23.4 1.0 NE A:ARG38 4.2 18.2 1.0 NE2 A:GLN68 4.2 31.4 1.0 CG A:LEU72 4.3 21.1 1.0 CD2 A:LEU72 4.3 21.7 1.0 O A:GLN68 4.3 28.2 1.0 CD1 A:LEU64 4.6 22.2 1.0 CG A:GLN68 4.7 27.2 1.0 CG A:ARG38 4.7 16.9 1.0 C A:GLN68 4.8 25.1 1.0 CB A:ARG38 4.8 17.9 1.0 CA A:GLN68 4.8 24.0 1.0 O A:HOH499 4.8 43.9 1.0 CD A:GLN68 4.8 35.5 1.0 CL A:CL205 5.0 37.4 0.8

Chlorine binding site 3 out of 3 in the Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Cour From Rhodococcus Jostii RHA1 Bound to P- Coumaroyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl203 b:31.5 occ:0.70 NE2 B:GLN55 2.9 43.5 1.0 O B:HOH527 3.0 38.2 1.0 O B:HOH489 3.1 41.9 1.0 NH2 B:ARG84 3.3 30.5 1.0 NE B:ARG84 3.4 29.3 1.0 CZ B:ARG84 3.8 28.7 1.0 CD B:GLN55 3.9 43.1 1.0 CG2 B:VAL73 3.9 19.1 1.0 CG B:GLN55 3.9 29.1 1.0 CB B:VAL73 4.0 19.2 1.0 CG1 B:VAL73 4.1 21.2 1.0 CA B:VAL70 4.2 23.0 1.0 CB B:GLN55 4.2 27.9 1.0 CD1 B:ILE96 4.4 23.6 1.0 CG2 B:VAL70 4.5 32.2 1.0 CG1 B:ILE96 4.5 22.7 1.0 CD B:ARG84 4.6 29.8 1.0 CB B:VAL70 4.8 29.6 1.0 O B:HOH459 4.8 48.1 1.0 N B:VAL70 4.8 22.5 1.0 O B:VAL70 4.9 22.6 1.0 CG1 B:VAL70 4.9 31.3 1.0 O B:ILE69 5.0 19.1 1.0

H.Otani, P.J.Stogios, X.Xu, B.Nocek, S.N.Li, A.Savchenko, L.D.Eltis. The Activity of Cour, A Marr Family Transcriptional Regulator, Is Modulated Through A Novel Molecular Mechanism. Nucleic Acids Res. V. 44 595 2016.
ISSN: ESSN 1362-4962
PubMed: 26400178
DOI: 10.1093/NAR/GKV955