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Chlorine in PDB 4wcb: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309Q

Enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309Q

All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309Q:
3.1.4.37;

Protein crystallography data

The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309Q, PDB code: 4wcb 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) 28.87 / 1.57
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.810, 48.270, 108.060, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 20.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309Q (pdb code 4wcb). 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 H309Q, PDB code: 4wcb:

Chlorine binding site 1 out of 1 in 4wcb

Go back to Chlorine Binding Sites List in 4wcb
Chlorine binding site 1 out of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309Q


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 H309Q within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:19.7
occ:1.00
 H A:SER297 2.3 19.8 1.0
HG A:SER297 2.4 29.8 1.0
HE1 A:TRP289 2.4 15.7 1.0
H A:GLY305 2.6 21.0 1.0
HD12 A:LEU293 3.0 22.0 1.0
OG A:SER297 3.1 24.8 1.0
N A:SER297 3.2 16.5 1.0
NE1 A:TRP289 3.2 13.1 1.0
HA A:PRO296 3.3 26.1 1.0
HG2 A:ARG307 3.3 21.6 1.0
HB2 A:SER297 3.3 21.5 1.0
HA A:PRO304 3.4 21.0 1.0
HD3 A:ARG307 3.4 19.3 1.0
O A:HOH566 3.5 18.4 1.0
N A:GLY305 3.5 17.5 1.0
O A:HOH535 3.6 20.5 1.0
CB A:SER297 3.6 17.9 1.0
HD1 A:TRP289 3.8 16.8 1.0
CD1 A:TRP289 3.9 14.0 1.0
CA A:PRO296 3.9 21.8 1.0
CD1 A:LEU293 4.0 18.4 1.0
CG A:ARG307 4.0 18.0 1.0
CA A:SER297 4.0 15.6 1.0
C A:PRO296 4.0 20.6 1.0
HB2 A:PRO296 4.1 26.8 1.0
HA2 A:GLY305 4.1 17.1 1.0
HG3 A:ARG307 4.1 21.6 1.0
CD A:ARG307 4.1 16.1 1.0
HB2 A:LEU293 4.1 23.6 1.0
CA A:PRO304 4.2 17.5 1.0
HD11 A:LEU293 4.3 22.0 1.0
HB3 A:PRO296 4.3 26.8 1.0
CE2 A:TRP289 4.3 10.6 1.0
HB3 A:PRO304 4.3 29.1 1.0
CB A:PRO296 4.3 22.3 1.0
CA A:GLY305 4.3 14.3 1.0
C A:PRO304 4.4 19.5 1.0
H A:ARG307 4.4 17.3 1.0
HZ2 A:TRP289 4.4 13.0 1.0
HG A:LEU293 4.5 22.8 1.0
H A:SER306 4.5 14.4 1.0
HD13 A:LEU293 4.5 22.0 1.0
H A:ALA298 4.5 21.6 1.0
HB3 A:SER297 4.5 21.5 1.0
HA A:SER297 4.6 18.7 1.0
HD2 A:ARG307 4.6 19.3 1.0
CG A:LEU293 4.7 19.0 1.0
CZ2 A:TRP289 4.8 10.8 1.0
CB A:PRO304 4.8 24.3 1.0
CB A:LEU293 4.9 19.7 1.0
O A:HOH586 4.9 31.8 1.0
N A:SER306 4.9 12.0 1.0
O A:PRO290 4.9 17.4 1.0
C A:GLY305 5.0 10.4 1.0

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 22:27:56 2025

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