2E48
Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme
Summary for 2E48
Entry DOI | 10.2210/pdb2e48/pdb |
Related | 2DU8 2E49 2E4A 2E82 |
Descriptor | D-amino-acid oxidase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
Functional Keywords | structurally ambivalent peptide, substrate-free holoenzyme, oxidoreductase |
Biological source | Homo sapiens (human) |
Cellular location | Peroxisome: P14920 |
Total number of polymer chains | 4 |
Total formula weight | 161225.84 |
Authors | Kawazoe, T.,Tsuge, H.,Imagawa, T.,Fukui, K. (deposition date: 2006-12-05, release date: 2007-03-06, Last modification date: 2023-10-25) |
Primary citation | Kawazoe, T.,Tsuge, H.,Imagawa, T.,Aki, K.,Kuramitsu, S.,Fukui, K. Structural basis of d-DOPA oxidation by d-amino acid oxidase: Alternative pathway for dopamine biosynthesis. Biochem.Biophys.Res.Commun., 355:385-391, 2007 Cited by PubMed: 17303072DOI: 10.1016/j.bbrc.2007.01.181 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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