Chlorine in PDB 4wdh: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168A

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168A:
3.1.4.37;

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168A, PDB code: 4wdh 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)	53.86 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.310, 48.330, 54.030, 90.00, 94.52, 90.00
R / Rfree (%)	21.7 / 25.9

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168A (pdb code 4wdh). 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 Y168A, PDB code: 4wdh:
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 Y168A


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 Y168A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:45.2 occ:1.00 H A:ALA260 2.5 32.7 1.0 HA A:LYS259 3.0 40.5 1.0 O A:HOH561 3.0 31.2 1.0 N A:ALA260 3.3 27.2 1.0 HD2 A:LYS259 3.3 46.2 1.0 HB3 A:LYS259 3.5 42.8 1.0 HB3 A:ALA260 3.5 38.0 1.0 HD3 A:LYS259 3.7 46.2 1.0 CA A:LYS259 3.7 33.7 1.0 O A:HOH550 3.7 49.9 1.0 HB2 A:ALA260 3.8 38.0 1.0 CD A:LYS259 3.9 38.5 1.0 CB A:ALA260 4.0 31.7 1.0 C A:LYS259 4.0 32.6 1.0 CB A:LYS259 4.0 35.7 1.0 CA A:ALA260 4.3 30.4 1.0 CG A:LYS259 4.6 36.6 1.0 O A:GLY258 4.7 25.9 1.0 HZ2 A:LYS259 4.8 51.0 1.0 HB2 A:LYS259 4.9 42.8 1.0 HB1 A:ALA260 4.9 38.0 1.0 N A:LYS259 5.0 29.9 1.0 HA A:ALA260 5.0 36.4 1.0 O A:ALA260 5.0 29.8 1.0

Chlorine binding site 2 out of 2 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation Y168A


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 Y168A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:41.1 occ:1.00 HE A:ARG182 2.3 46.5 1.0 HG A:SER178 2.5 32.1 1.0 HH21 A:ARG182 2.7 45.8 1.0 NE A:ARG182 3.1 38.8 1.0 OG A:SER178 3.1 26.8 1.0 HG2 A:GLU179 3.3 39.2 0.5 HB3 A:SER178 3.3 35.6 1.0 NH2 A:ARG182 3.5 38.2 1.0 HG3 A:GLU179 3.5 38.6 0.5 HA A:VAL228 3.6 27.3 1.0 HA A:GLU179 3.6 32.7 0.5 HA A:GLU179 3.6 31.1 0.5 O A:HOH569 3.6 39.7 1.0 CD A:GLU179 3.7 33.1 0.5 CZ A:ARG182 3.7 40.4 1.0 CB A:SER178 3.8 29.7 1.0 OE2 A:GLU179 3.9 34.6 0.5 CG A:GLU179 3.9 32.7 0.5 N A:GLU179 4.0 27.5 0.5 HD2 A:ARG182 4.0 40.2 1.0 N A:GLU179 4.0 27.6 0.5 OE1 A:GLU179 4.0 34.3 0.5 HG2 A:GLU179 4.0 38.6 0.5 C A:SER178 4.0 25.9 1.0 CD A:ARG182 4.2 33.5 1.0 H A:GLU179 4.2 33.0 0.5 CG A:GLU179 4.2 32.2 0.5 H A:GLU179 4.2 33.1 0.5 CA A:GLU179 4.2 27.2 0.5 HH22 A:ARG182 4.2 45.8 1.0 O A:SER178 4.2 25.4 1.0 CA A:GLU179 4.2 25.9 0.5 HB2 A:ARG182 4.3 34.2 1.0 H A:LEU229 4.3 29.6 1.0 HG11 A:VAL228 4.3 28.3 1.0 HG A:LEU229 4.4 21.1 1.0 HG2 A:LYS175 4.5 60.1 1.0 HB2 A:SER178 4.5 35.6 1.0 CA A:SER178 4.5 26.1 1.0 CA A:VAL228 4.6 22.7 1.0 HB3 A:ARG182 4.6 34.2 1.0 O A:GLY227 4.6 44.2 1.0 CB A:GLU179 4.7 30.8 0.5 HG3 A:GLU179 4.7 39.2 0.5 O A:LYS175 4.7 42.0 1.0 HD3 A:ARG182 4.8 40.2 1.0 CB A:ARG182 4.8 28.5 1.0 CB A:GLU179 4.8 31.1 0.5 HA A:LYS175 4.8 52.2 1.0 HG13 A:VAL228 4.9 28.3 1.0 N A:LEU229 5.0 24.7 1.0 CG1 A:VAL228 5.0 23.6 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