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Atomistry » Chlorine » PDB 4hw3-4i1y » 4hzo | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4hw3-4i1y » 4hzo » |
Chlorine in PDB 4hzo: The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog FoldProtein crystallography data
The structure of The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold, PDB code: 4hzo
was solved by
J.R.Lohman,
C.A.Bingman,
G.N.Phillips Jr.,
B.Shen,
Enzyme Discovery Fornatural Product Biosynthesis (Natpro),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold
(pdb code 4hzo). 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 The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold, PDB code: 4hzo: Chlorine binding site 1 out of 1 in 4hzoGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the The Structure of the Bifunctional Acetyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double Hot Dog Fold
![]() Mono view ![]() Stereo pair view
Reference:
J.R.Lohman,
C.A.Bingman,
G.N.Phillips,
B.Shen.
Structure of the Bifunctional Acyltransferase/Decarboxylase Lnmk From the Leinamycin Biosynthetic Pathway Revealing Novel Activity For A Double-Hot-Dog Fold. Biochemistry V. 52 902 2013.
Page generated: Fri Jul 11 16:36:55 2025
ISSN: ISSN 0006-2960 PubMed: 23320975 DOI: 10.1021/BI301652Y |
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