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Atomistry » Chlorine » PDB 5u7k-5ufo » 5ub9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5u7k-5ufo » 5ub9 » |
Chlorine in PDB 5ub9: Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter JejuniEnzymatic activity of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni
All present enzymatic activity of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni:
2.4.2.17; Protein crystallography data
The structure of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni, PDB code: 5ub9
was solved by
G.Mittelstaedt,
W.Jiao,
E.K.Livingstone,
E.J.Parker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ub9:
The structure of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni
(pdb code 5ub9). 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 Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni, PDB code: 5ub9: Chlorine binding site 1 out of 1 in 5ub9Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni
![]() Mono view ![]() Stereo pair view
Reference:
G.Mittelstadt,
W.Jiao,
E.K.Livingstone,
G.J.Moggre,
A.R.Nazmi,
E.J.Parker.
A Dimeric Catalytic Core Relates the Short and Long Forms of Atp-Phosphoribosyltransferase. Biochem. J. V. 475 247 2018.
Page generated: Sat Jul 12 09:17:59 2025
ISSN: ESSN 1470-8728 PubMed: 29208762 DOI: 10.1042/BCJ20170762 |
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