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Chlorine in PDB 4wca: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate

Enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate:
3.1.4.37;

Protein crystallography data

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate, PDB code: 4wca 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) 19.62 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.430, 47.640, 107.650, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate (pdb code 4wca). 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 Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate, PDB code: 4wca:

Chlorine binding site 1 out of 1 in 4wca

Go back to Chlorine Binding Sites List in 4wca
Chlorine binding site 1 out of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H230Q, Complexed with Citrate


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 H230Q, Complexed with Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:42.2
occ:1.00
 HE A:ARG182 2.1 33.4 1.0
HZ1 A:LYS175 2.6 61.4 1.0
HG A:SER178 2.7 20.2 0.7
NE A:ARG182 2.9 27.8 1.0
HB3 A:SER178 3.0 23.0 0.3
HB3 A:SER178 3.2 20.7 0.7
OG A:SER178 3.2 16.9 0.7
HD2 A:ARG182 3.3 33.6 1.0
HH21 A:ARG182 3.4 35.5 1.0
HG3 A:GLU179 3.5 38.5 1.0
NZ A:LYS175 3.5 51.2 1.0
HA A:GLU179 3.6 29.7 1.0
HB2 A:SER178 3.6 23.0 0.3
O A:GLY227 3.7 33.2 1.0
CD A:ARG182 3.7 28.0 1.0
HG2 A:GLU179 3.7 38.5 1.0
CB A:SER178 3.7 17.2 0.7
CB A:SER178 3.7 19.1 0.3
HZ3 A:LYS175 3.7 61.4 1.0
HA A:VAL228 3.7 27.9 1.0
HD2 A:LYS175 3.8 56.0 1.0
HG3 A:ARG182 3.9 36.8 1.0
CZ A:ARG182 3.9 30.1 1.0
N A:GLU179 3.9 21.1 1.0
NH2 A:ARG182 4.0 29.6 1.0
C A:SER178 4.0 19.4 0.7
C A:SER178 4.0 19.7 0.3
HZ2 A:LYS175 4.0 61.4 1.0
CG A:GLU179 4.0 32.1 1.0
HE3 A:LYS175 4.0 52.4 1.0
H A:GLU179 4.1 25.4 0.3
H A:GLU179 4.1 25.4 0.7
O A:SER178 4.2 17.9 0.3
CA A:GLU179 4.2 24.8 1.0
O A:SER178 4.2 19.5 0.7
CE A:LYS175 4.2 43.7 1.0
CG A:ARG182 4.3 30.7 1.0
HG A:LEU229 4.3 20.5 1.0
HB2 A:ARG182 4.4 28.8 1.0
CD A:LYS175 4.5 46.6 1.0
CA A:SER178 4.5 19.6 0.7
H A:LEU229 4.5 19.5 1.0
HD3 A:ARG182 4.5 33.6 1.0
HB2 A:SER178 4.5 20.7 0.7
CA A:SER178 4.5 19.7 0.3
HG12 A:VAL228 4.6 29.9 1.0
CA A:VAL228 4.7 23.2 1.0
CB A:GLU179 4.7 27.6 1.0
C A:GLY227 4.8 28.8 1.0
HH22 A:ARG182 4.8 35.5 1.0
OG A:SER178 4.8 16.1 0.3
O A:LYS175 4.8 27.9 1.0
CB A:ARG182 4.9 24.0 1.0
HA A:SER178 5.0 23.5 0.7

Reference:

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
Page generated: Fri Jul 11 22:27:55 2025

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