7ODC

CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM RESOLUTION

Summary for 7ODC

Entry DOI	10.2210/pdb7odc/pdb
Descriptor	PROTEIN (ORNITHINE DECARBOXYLASE), PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
Functional Keywords	pyridoxal-5'-phosphate, plp, group iv decarboxylase, polyamines, parasitical, chemotherapy target, ornithine, putrescine, a/b-barrel, obligate, lyase
Biological source	Mus musculus (house mouse)
Total number of polymer chains	1
Total formula weight	47522.94
Authors	Kern, A.D.,Oliveira, M.A.,Coffino, P.,Hackert, M.L. (deposition date: 1999-03-03, release date: 1999-10-22, Last modification date: 2023-12-27)
Primary citation	Kern, A.D.,Oliveira, M.A.,Coffino, P.,Hackert, M.L. Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure Fold.Des., 7:567-581, 1999 Cited by PubMed Abstract: Pyridoxal-5'-phosphate (PLP) dependent enzymes catalyze a broad range of reactions, resulting in bond cleavage at C alpha, C beta, or C gamma carbons of D and L amino acid substrates. Ornithine decarboxylase (ODC) is a PLP-dependent enzyme that controls a critical step in the biosynthesis of polyamines, small organic polycations whose controlled levels are essential for proper growth. ODC inhibition has applications for the treatment of certain cancers and parasitic ailments such as African sleeping sickness. PubMed: 10378276 DOI: 10.1016/S0969-2126(99)80073-2 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation