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Chlorine in PDB 5ubg: Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni with Bound Phosphoribosyl-AtpEnzymatic activity of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni with Bound Phosphoribosyl-Atp
All present enzymatic activity of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni with Bound Phosphoribosyl-Atp:
2.4.2.17; Protein crystallography data
The structure of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni with Bound Phosphoribosyl-Atp, PDB code: 5ubg
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 5ubg:
The structure of Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni with Bound Phosphoribosyl-Atp 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 with Bound Phosphoribosyl-Atp
(pdb code 5ubg). 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 with Bound Phosphoribosyl-Atp, PDB code: 5ubg: Chlorine binding site 1 out of 1 in 5ubgGo back to Chlorine Binding Sites List in 5ubg
Chlorine binding site 1 out
of 1 in the Catalytic Core Domain of Adenosine Triphosphate Phosphoribosyltransferase From Campylobacter Jejuni with Bound Phosphoribosyl-Atp
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 Dec 12 12:30:53 2020
ISSN: ESSN 1470-8728 PubMed: 29208762 DOI: 10.1042/BCJ20170762 |
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