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4HZO

The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double Hot Dog Fold

Summary for 4HZO
Entry DOI10.2210/pdb4hzo/pdb
Related4HZN
DescriptorBifunctional methylmalonyl-CoA:ACP acyltransferase/decarboxylase, CHLORIDE ION, COENZYME A, ... (4 entities in total)
Functional Keywordsstructural genomics, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, psi-biology, double hot dog fold, acyl carrier protein - lnml, transferase, lyase
Biological sourceStreptomyces atroolivaceus
Total number of polymer chains1
Total formula weight36082.27
Authors
Lohman, J.R.,Bingman, C.A.,Phillips Jr., G.N.,Shen, B.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2012-11-15, release date: 2013-01-30, Last modification date: 2024-02-28)
Primary citationLohman, J.R.,Bingman, C.A.,Phillips, G.N.,Shen, B.
Structure of the Bifunctional Acyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double-Hot-Dog Fold.
Biochemistry, 52:902-911, 2013
Cited by
PubMed: 23320975
DOI: 10.1021/bi301652y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.76 Å)
Structure validation

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