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Atomistry » Chlorine » PDB 2yj9-2yz7 » 2ype | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2yj9-2yz7 » 2ype » |
Chlorine in PDB 2ype: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic AmpEnzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp
All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp:
3.1.4.37; Protein crystallography data
The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp, PDB code: 2ype
was solved by
M.Myllykoski,
A.Raasakka,
M.Lehtimaki,
H.Han,
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 H309S, Crystallized with 2',3'- Cyclic Amp
(pdb code 2ype). 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 H309S, Crystallized with 2',3'- Cyclic Amp, PDB code: 2ype: Chlorine binding site 1 out of 1 in 2ypeGo back to Chlorine Binding Sites List in 2ype
Chlorine binding site 1 out
of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation H309S, Crystallized with 2',3'- Cyclic Amp
Mono view Stereo pair view
Reference:
M.Myllykoski,
A.Raasakka,
M.Lehtimaki,
H.Han,
I.Kursula,
P.Kursula.
Crystallographic Analysis of the Reaction Cycle of 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase, A Unique Member of the 2H Phosphoesterase Family J.Mol.Biol. V. 425 4307 2013.
Page generated: Sat Dec 12 09:29:43 2020
ISSN: ISSN 0022-2836 PubMed: 23831225 DOI: 10.1016/J.JMB.2013.06.012 |
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