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Atomistry » Chlorine » PDB 4hw2-4i1u » 4hzp | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4hw2-4i1u » 4hzp » |
Chlorine in PDB 4hzp: 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: 4hzp
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 4hzp). 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: 4hzp: Chlorine binding site 1 out of 1 in 4hzpGo back to Chlorine Binding Sites List in 4hzp
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: Sat Dec 12 10:44:10 2020
ISSN: ISSN 0006-2960 PubMed: 23320975 DOI: 10.1021/BI301652Y |
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