6J0Z
Crystal structure of AlpK
Summary for 6J0Z
Entry DOI | 10.2210/pdb6j0z/pdb |
Descriptor | Putative angucycline-like polyketide oxygenase, FLAVIN-ADENINE DINUCLEOTIDE (2 entities in total) |
Functional Keywords | putative oxygenase, fad-binding, oxidoreductase |
Biological source | Streptomyces ambofaciens |
Total number of polymer chains | 1 |
Total formula weight | 53105.74 |
Authors | |
Primary citation | Wang, W.,Li, J.,Li, H.,Fan, K.,Liu, Y. Crystal structure of AlpK: An essential monooxygenase involved in the biosynthesis of kinamycin Biochem. Biophys. Res. Commun., 510:601-605, 2019 Cited by PubMed Abstract: AlpK is an essential monooxygenase involved in the biosynthesis of kinamycin. It catalyzes the C5-hyfroxylattion of the crucial benzo[b]-fluorence intermediate in kinamycin synthesis. However, the structure and mechanism of AlpK is unclear. Here, we report the first structure of AlpK in complex with FAD. Our structure sheds light on the catalytic mechanism of AlpK. PubMed: 30739782DOI: 10.1016/j.bbrc.2019.01.077 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.889 Å) |
Structure validation
Download full validation report
