4HZP
The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double Hot Dog Fold
Summary for 4HZP
Entry DOI | 10.2210/pdb4hzp/pdb |
Related | 4HZN 4HZO |
Descriptor | Bifunctional methylmalonyl-CoA:ACP Acyltransferase/Decarboxylase, COENZYME A, CHLORIDE ION, ... (5 entities in total) |
Functional Keywords | structural genomics, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, psi-biology, double hot dog fold, acyl carrier protein - lnml, methylmalonyl-coa, transferase, lyase |
Biological source | Streptomyces atroolivaceus |
Total number of polymer chains | 1 |
Total formula weight | 36258.40 |
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: 2023-09-20) |
Primary citation | Lohman, 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: 23320975DOI: 10.1021/bi301652y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
Download full validation report