Chlorine in PDB 5ae0: Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution

All present enzymatic activity of Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution:
3.1.4.37;

The structure of Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution, PDB code: 5ae0 was solved by S.Laulumaa, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.29 / 1.04
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.650, 47.560, 51.220, 90.00, 97.51, 90.00
R / Rfree (%)	12.7 / 15.6

The binding sites of Chlorine atom in the Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution (pdb code 5ae0). 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 Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution, PDB code: 5ae0:

Chlorine binding site 1 out of 1 in the Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Perdeuterated Mouse Cnpase Catalytic Domain at Atomic Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1380 b:18.9 occ:0.73 O A:HOH2204 2.2 28.0 1.0 D A:ARG307 2.3 8.5 1.0 D A:GLY305 2.6 11.5 1.0 O A:HOH2130 2.6 45.3 1.0 O A:HOH2210 2.9 27.8 1.0 O A:HOH2203 3.0 26.6 1.0 DB2 A:ARG307 3.0 12.1 1.0 D A:SER306 3.0 9.0 1.0 DE1 A:TRP289 3.1 14.4 1.0 N A:ARG307 3.1 7.1 1.0 N A:GLY305 3.2 9.6 1.0 DB3 A:ARG307 3.3 12.1 1.0 N A:SER306 3.3 7.5 1.0 DD21 A:LEU328 3.5 11.2 1.0 DB2 A:SER306 3.5 10.6 1.0 CB A:ARG307 3.5 10.1 1.0 DA A:PRO304 3.7 19.2 1.0 C A:GLY305 3.7 7.6 1.0 NE1 A:TRP289 3.7 12.0 1.0 DA2 A:GLY305 3.7 10.1 1.0 CA A:GLY305 3.8 8.4 1.0 CA A:ARG307 4.0 7.2 1.0 CA A:SER306 4.0 7.9 1.0 C A:SER306 4.0 7.7 1.0 C A:PRO304 4.1 11.4 1.0 DZ2 A:TRP289 4.2 14.0 1.0 O A:PRO303 4.2 11.8 1.0 CB A:SER306 4.2 8.8 1.0 CA A:PRO304 4.4 16.0 1.0 O A:HOH2220 4.4 34.1 1.0 CE2 A:TRP289 4.4 10.4 1.0 CD2 A:LEU328 4.4 9.3 1.0 DD11 A:LEU328 4.5 12.4 1.0 O A:HOH2207 4.5 39.7 1.0 DD2 A:ARG307 4.6 17.0 1.0 DA A:ARG307 4.6 8.7 1.0 DD22 A:LEU328 4.6 11.2 1.0 O A:GLY305 4.6 8.1 1.0 CZ2 A:TRP289 4.6 11.7 1.0 CD1 A:TRP289 4.6 12.0 1.0 DB2 A:SER299 4.7 32.0 1.0 DA3 A:GLY305 4.7 10.1 1.0 DD3 A:ARG307 4.7 17.0 1.0 D A:ALA308 4.8 7.0 1.0 DD1 A:TRP289 4.8 14.4 1.0 DG A:SER306 4.8 13.3 1.0 CG A:ARG307 4.8 10.1 1.0 DB3 A:SER306 4.9 10.6 1.0 DD23 A:LEU328 4.9 11.2 1.0 CD A:ARG307 4.9 14.2 1.0 DA A:SER306 4.9 9.5 1.0

A.Raasakka, M.Myllykoski, S.Laulumaa, M.Lehtimaki, M.Hartlein, M.Moulin, I.Kursula, P.Kursula. Determinants of Ligand Binding and Catalytic Activity in the Myelin Enzyme 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase. Sci Rep V. 5 16520 2015.
ISSN: ESSN 2045-2322
PubMed: 26563764
DOI: 10.1038/SREP16520