Chlorine in PDB 5t3n: Sp-2CL-Camps Bound to Pkar CBD2

All present enzymatic activity of Sp-2CL-Camps Bound to Pkar CBD2:
2.7.11.11;

The structure of Sp-2CL-Camps Bound to Pkar CBD2, PDB code: 5t3n was solved by D.R.Littler, P.Gilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.42 / 2.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.190, 64.190, 195.710, 90.00, 90.00, 90.00
R / Rfree (%)	25.1 / 30.7

The structure of Sp-2CL-Camps Bound to Pkar CBD2 also contains other interesting chemical elements:

Iodine

(I)

5 atoms

The binding sites of Chlorine atom in the Sp-2CL-Camps Bound to Pkar CBD2 (pdb code 5t3n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Sp-2CL-Camps Bound to Pkar CBD2, PDB code: 5t3n:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Sp-2CL-Camps Bound to Pkar CBD2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Sp-2CL-Camps Bound to Pkar CBD2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:0.2 occ:1.00 CL1 A:75G503 0.0 0.2 1.0 C1 A:75G503 1.8 49.7 1.0 N4 A:75G503 2.7 49.1 1.0 N5 A:75G503 2.7 52.0 1.0 CD2 A:LEU378 3.4 66.0 1.0 CB A:ALA387 3.6 63.8 1.0 CG1 A:ILE438 3.7 89.5 1.0 CD1 A:ILE438 3.8 86.5 1.0 CD1 A:LEU428 3.9 58.1 1.0 C2 A:75G503 4.0 51.0 1.0 C4 A:75G503 4.0 51.9 1.0 SG A:CYS437 4.0 0.2 1.0 C3 A:75G503 4.4 52.2 1.0 S1 A:75G503 4.6 65.7 1.0 CD2 A:TYR424 4.7 61.0 1.0 CB A:TYR424 4.8 62.6 1.0 CG A:TYR424 4.9 60.1 1.0 CG A:LEU378 4.9 63.2 1.0 CA A:ALA387 4.9 68.9 1.0

Chlorine binding site 2 out of 2 in the Sp-2CL-Camps Bound to Pkar CBD2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Sp-2CL-Camps Bound to Pkar CBD2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl504 b:0.4 occ:1.00 CL1 B:75G504 0.0 0.4 1.0 C1 B:75G504 1.7 80.5 1.0 N4 B:75G504 2.7 78.8 1.0 N5 B:75G504 2.7 79.7 1.0 CB B:ALA387 3.6 88.1 1.0 CD1 B:LEU428 3.7 90.1 1.0 SG B:CYS437 3.8 0.9 1.0 C2 B:75G504 3.9 78.8 1.0 C4 B:75G504 3.9 81.0 1.0 CD2 B:LEU378 4.0 0.5 1.0 CD1 B:ILE438 4.2 89.5 1.0 C3 B:75G504 4.4 80.2 1.0 CG1 B:ILE438 4.5 94.4 1.0 CB B:TYR424 4.5 94.5 1.0 CG B:LEU428 4.6 85.4 1.0 CD2 B:LEU428 4.7 84.3 1.0 O B:ALA387 4.8 89.8 1.0 CA B:ALA387 4.8 88.0 1.0 C B:ALA387 4.9 86.1 1.0 CG B:TYR424 4.9 89.8 1.0 CD2 B:TYR424 5.0 91.5 1.0

D.R.Littler, H.E.Bullen, K.L.Harvey, T.Beddoe, B.S.Crabb, J.Rossjohn, P.R.Gilson. Disrupting the Allosteric Interaction Between the Plasmodium Falciparum Camp-Dependent Kinase and Its Regulatory Subunit. J. Biol. Chem. V. 291 25375 2016.
ISSN: ESSN 1083-351X
PubMed: 27738107
DOI: 10.1074/JBC.M116.750174