Chlorine in PDB 4wbl: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A:
3.1.4.37;

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A, PDB code: 4wbl was solved by M.Myllykoski, A.Raasakka, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.44 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	40.220, 47.770, 54.090, 90.00, 94.73, 90.00
R / Rfree (%)	19.5 / 26.5

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A (pdb code 4wbl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A, PDB code: 4wbl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:49.7 occ:1.00 H A:ARG307 2.4 43.8 1.0 H A:GLY305 2.7 41.4 1.0 HB3 A:ARG307 2.9 46.5 1.0 H A:SER306 2.9 36.7 1.0 HB2 A:ARG307 3.0 46.5 1.0 HZ2 A:LYS295 3.1 0.7 1.0 HE1 A:TRP289 3.2 47.2 1.0 N A:ARG307 3.2 36.5 1.0 N A:GLY305 3.3 34.5 1.0 N A:SER306 3.3 30.6 1.0 HD21 A:LEU328 3.3 40.8 1.0 CB A:ARG307 3.4 38.7 1.0 HB2 A:SER299 3.5 97.6 1.0 HB2 A:SER306 3.6 37.2 1.0 HA A:PRO304 3.7 51.3 1.0 HA2 A:GLY305 3.7 38.2 1.0 C A:GLY305 3.8 29.7 1.0 NE1 A:TRP289 3.8 39.3 1.0 CA A:GLY305 3.8 31.8 1.0 CA A:ARG307 3.9 35.8 1.0 NZ A:LYS295 3.9 94.7 1.0 HZ2 A:TRP289 4.0 48.0 1.0 HZ3 A:LYS295 4.0 0.7 1.0 CA A:SER306 4.1 29.1 1.0 C A:SER306 4.1 27.7 1.0 HZ1 A:LYS295 4.1 0.7 1.0 HD11 A:LEU328 4.1 40.6 1.0 C A:PRO304 4.1 38.2 1.0 CD2 A:LEU328 4.2 34.0 1.0 CB A:SER306 4.3 31.0 1.0 HD22 A:LEU328 4.4 40.8 1.0 CA A:PRO304 4.4 42.7 1.0 CE2 A:TRP289 4.4 38.5 1.0 CB A:SER299 4.4 81.4 1.0 HB3 A:SER299 4.4 97.6 1.0 CZ2 A:TRP289 4.5 40.0 1.0 HA A:ARG307 4.5 43.0 1.0 O A:PRO303 4.5 36.6 1.0 HD2 A:ARG307 4.5 51.2 1.0 HD3 A:ARG307 4.5 51.2 1.0 H A:ALA308 4.6 38.3 1.0 CG A:ARG307 4.7 39.1 1.0 O A:GLY305 4.7 27.7 1.0 CD1 A:TRP289 4.7 37.8 1.0 HA3 A:GLY305 4.7 38.2 1.0 HD23 A:LEU328 4.8 40.8 1.0 CD A:ARG307 4.8 42.7 1.0 HD1 A:TRP289 4.9 45.4 1.0 CD1 A:LEU328 4.9 33.9 1.0 OG A:SER306 5.0 32.6 1.0 HA A:SER299 5.0 96.0 1.0 HA A:SER306 5.0 35.0 1.0

Chlorine binding site 2 out of 2 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation F235A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:51.5 occ:1.00 HE A:ARG182 2.6 36.3 0.5 HB3 A:SER178 2.7 43.4 1.0 HG2 A:GLU179 3.0 56.5 1.0 HH12 A:ARG182 3.1 33.9 0.5 HD2 A:ARG182 3.2 33.6 0.5 HB2 A:SER178 3.2 43.4 1.0 CB A:SER178 3.4 36.1 1.0 NE A:ARG182 3.4 30.2 0.5 HG3 A:GLU179 3.4 56.5 1.0 HA A:GLU179 3.4 46.8 1.0 HD3 A:ARG182 3.5 34.2 0.5 HZ3 A:LYS175 3.5 67.4 1.0 NH1 A:ARG182 3.5 28.2 0.5 HA A:VAL228 3.5 36.2 1.0 CG A:GLU179 3.6 47.1 1.0 N A:GLU179 3.7 37.4 1.0 C A:SER178 3.7 31.5 1.0 HH11 A:ARG182 3.8 33.9 0.5 O A:GLY227 3.8 55.5 1.0 HH21 A:ARG182 3.9 40.7 0.5 H A:GLU179 3.9 44.9 1.0 O A:SER178 3.9 28.6 1.0 CA A:GLU179 4.0 39.0 1.0 HB2 A:ARG182 4.0 32.0 0.5 CD A:ARG182 4.0 28.5 0.5 HG A:LEU229 4.0 28.5 1.0 HB2 A:ARG182 4.1 32.0 0.5 CD A:ARG182 4.1 28.0 0.5 HB3 A:ARG182 4.2 32.0 0.5 CA A:SER178 4.2 33.8 1.0 CZ A:ARG182 4.2 26.7 0.5 HB3 A:ARG182 4.3 32.0 0.5 HE3 A:LYS175 4.3 67.5 1.0 NZ A:LYS175 4.3 56.2 1.0 H A:LEU229 4.3 35.8 1.0 HZ2 A:LYS175 4.4 67.4 1.0 CZ A:ARG182 4.4 32.1 0.5 CB A:GLU179 4.4 43.4 1.0 HG A:SER178 4.4 43.8 1.0 HD2 A:LYS175 4.5 64.0 1.0 CA A:VAL228 4.5 30.2 1.0 NE A:ARG182 4.5 26.5 0.5 NH2 A:ARG182 4.5 33.9 0.5 C A:GLY227 4.5 53.5 1.0 OG A:SER178 4.5 36.5 1.0 CB A:ARG182 4.5 26.7 0.5 CB A:ARG182 4.5 26.7 0.5 HG12 A:VAL228 4.5 39.0 1.0 HD3 A:ARG182 4.6 33.6 0.5 HD2 A:ARG182 4.7 34.2 0.5 CE A:LYS175 4.7 56.2 1.0 HA A:SER178 4.8 40.5 1.0 O A:LYS175 4.8 38.9 1.0 N A:VAL228 4.8 30.4 1.0 CD A:GLU179 4.8 53.4 1.0 N A:LEU229 4.9 29.9 1.0 OE2 A:GLU179 4.9 55.0 1.0 CG A:ARG182 4.9 27.5 0.5 CG A:ARG182 4.9 27.3 0.5 HD21 A:LEU229 4.9 28.3 1.0 HZ1 A:LYS175 5.0 67.4 1.0 CG A:LEU229 5.0 23.8 1.0 HB3 A:GLU179 5.0 52.1 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