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Atomistry » Chlorine » PDB 4v3y-4wcu » 4wcb | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4v3y-4wcu » 4wcb » |
Chlorine in PDB 4wcb: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309QEnzymatic 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:
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 4wcbGo back to![]() ![]()
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
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.
Page generated: Fri Jul 26 02:49:26 2024
ISSN: ESSN 2045-2322 PubMed: 26563764 DOI: 10.1038/SREP16520 |
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