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Atomistry » Arsenic » PDB 6i5n-6wr9 » 6rcx | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Arsenic » PDB 6i5n-6wr9 » 6rcx » |
Arsenic in PDB 6rcx: Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc.Enzymatic activity of Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc.
All present enzymatic activity of Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc.:
2.3.1.41; Protein crystallography data
The structure of Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc., PDB code: 6rcx
was solved by
M.C.Nguyen,
L.Mourey,
J.D.Pedelacq,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6rcx:
The structure of Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc. also contains other interesting chemical elements:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc.
(pdb code 6rcx). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc., PDB code: 6rcx: Arsenic binding site 1 out of 1 in 6rcxGo back to Arsenic Binding Sites List in 6rcx
Arsenic binding site 1 out
of 1 in the Mycobacterial 4'-Phosphopantetheinyl Transferase Pptab in Complex with the Acp Domain of Ppsc.
Mono view Stereo pair view
Reference:
M.C.Nguyen,
O.Saurel,
C.Carivenc,
S.Gavalda,
S.Saitta,
M.P.Tran,
A.Milon,
C.Chalut,
C.Guilhot,
L.Mourey,
J.D.Pedelacq.
Conformational Flexibility of Coenzyme A and Its Impact on the Post-Translational Modification of Acyl Carrier Proteins By 4'-Phosphopantetheinyl Transferases. Febs J. 2020.
Page generated: Sat Dec 12 01:49:38 2020
ISSN: ISSN 1742-464X PubMed: 32128972 DOI: 10.1111/FEBS.15273 |
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