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Atomistry » Chlorine » PDB 3x20-3zh8 » 3zbs | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3x20-3zh8 » 3zbs » |
Chlorine in PDB 3zbs: Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation V321A, Crystallized with 2'-AmpsEnzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation V321A, Crystallized with 2'-Amps
All present enzymatic activity of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation V321A, Crystallized with 2'-Amps:
3.1.4.37; Protein crystallography data
The structure of Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation V321A, Crystallized with 2'-Amps, PDB code: 3zbs
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 V321A, Crystallized with 2'-Amps
(pdb code 3zbs). 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 V321A, Crystallized with 2'-Amps, PDB code: 3zbs: Chlorine binding site 1 out of 1 in 3zbsGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Catalytic Domain of Mouse 2',3'-Cyclic Nucleotide 3'- Phosphodiesterase, with Mutation V321A, Crystallized with 2'-Amps
![]() 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: Fri Jul 11 12:13:07 2025
ISSN: ISSN 0022-2836 PubMed: 23831225 DOI: 10.1016/J.JMB.2013.06.012 |
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