4CWD

CRYSTAL STRUCTURE OF HUMAN GAMMA-BUTYROBETAINE,2-OXOGLUTARATE IN COMPLEX WITH 449, A NOVEL SUBSTRATE

Summary for 4CWD

Entry DOI	10.2210/pdb4cwd/pdb
Descriptor	GAMMA-BUTYROBETAINE DIOXYGENASE, NICKEL (II) ION, ZINC ION, ... (7 entities in total)
Functional Keywords	oxidoreductase, 2-og and iron dependent dioxygenase, carnitine biosynthesis
Biological source	Homo sapiens (Human)
Cellular location	Cytoplasm: O75936
Total number of polymer chains	1
Total formula weight	45397.47
Authors	McDonough, M.A.,Kochan, G.,Rydzik, A.,Schofield, C.J. (deposition date: 2014-04-02, release date: 2014-09-17, Last modification date: 2023-12-20)
Primary citation	Rydzik, A.M.,Leung, I.K.,Kochan, G.T.,McDonough, M.A.,Claridge, T.D.,Schofield, C.J. Oxygenase-catalyzed desymmetrization of N,N-dialkyl-piperidine-4-carboxylic acids. Angew. Chem. Int. Ed. Engl., 53:10925-10927, 2014 Cited by PubMed Abstract: γ-Butyrobetaine hydroxylase (BBOX) is a 2-oxoglutarate dependent oxygenase that catalyzes the final hydroxylation step in the biosynthesis of carnitine. BBOX was shown to catalyze the oxidative desymmetrization of achiral N,N-dialkyl piperidine-4-carboxylates to give products with two or three stereogenic centers. PubMed: 25164544 DOI: 10.1002/anie.201406125 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.899 Å)

Structure validation