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Atomistry » Chlorine » PDB 5cu4-5d0v » 5d08 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5cu4-5d0v » 5d08 » |
Chlorine in PDB 5d08: Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine ReductaseEnzymatic activity of Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase
All present enzymatic activity of Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase:
1.17.99.6; Protein crystallography data
The structure of Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase, PDB code: 5d08
was solved by
D.P.Dowling,
Z.D.Miles,
C.Kohrer,
V.Bandarian,
C.L.Drennan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5d08:
The structure of Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase
(pdb code 5d08). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase, PDB code: 5d08: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 5d08Go back to Chlorine Binding Sites List in 5d08
Chlorine binding site 1 out
of 2 in the Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 5d08Go back to Chlorine Binding Sites List in 5d08
Chlorine binding site 2 out
of 2 in the Crystal Structure of Selenomethionine-Labeled Epoxyqueuosine Reductase
Mono view Stereo pair view
Reference:
D.P.Dowling,
Z.D.Miles,
C.Kohrer,
S.J.Maiocco,
S.J.Elliott,
V.Bandarian,
C.L.Drennan.
Molecular Basis of Cobalamin-Dependent Rna Modification. Nucleic Acids Res. V. 44 9965 2016.
Page generated: Fri Jul 26 06:26:39 2024
ISSN: ESSN 1362-4962 PubMed: 27638883 DOI: 10.1093/NAR/GKW806 |
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