7ODC
CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM RESOLUTION
7ODC の概要
エントリーDOI | 10.2210/pdb7odc/pdb |
分子名称 | PROTEIN (ORNITHINE DECARBOXYLASE), PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
機能のキーワード | pyridoxal-5'-phosphate, plp, group iv decarboxylase, polyamines, parasitical, chemotherapy target, ornithine, putrescine, a/b-barrel, obligate, lyase |
由来する生物種 | Mus musculus (house mouse) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 47522.94 |
構造登録者 | Kern, A.D.,Oliveira, M.A.,Coffino, P.,Hackert, M.L. (登録日: 1999-03-03, 公開日: 1999-10-22, 最終更新日: 2023-12-27) |
主引用文献 | 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: 10378276DOI: 10.1016/S0969-2126(99)80073-2 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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