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Chlorine in PDB 5llx: Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp BoundEnzymatic activity of Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound
All present enzymatic activity of Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound:
2.7.7.65; Protein crystallography data
The structure of Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound, PDB code: 5llx
was solved by
G.Gourinchas,
A.Winkler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5llx:
The structure of Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound
(pdb code 5llx). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound, PDB code: 5llx: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 5llxGo back to Chlorine Binding Sites List in 5llx
Chlorine binding site 1 out
of 2 in the Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 5llxGo back to Chlorine Binding Sites List in 5llx
Chlorine binding site 2 out
of 2 in the Bacteriophytochrome Activated Diguanylyl Cyclase From Idiomarina Species A28L with Gtp Bound
Mono view Stereo pair view
Reference:
G.Gourinchas,
S.Etzl,
C.Gobl,
U.Vide,
T.Madl,
A.Winkler.
Long-Range Allosteric Signaling in Red Light-Regulated Diguanylyl Cyclases. Sci Adv V. 3 02498 2017.
Page generated: Sat Dec 12 12:03:33 2020
ISSN: ESSN 2375-2548 PubMed: 28275738 DOI: 10.1126/SCIADV.1602498 |
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