1C0L
D-AMINO ACID OXIDASE: STRUCTURE OF SUBSTRATE COMPLEXES AT VERY HIGH RESOLUTION REVEAL THE CHEMICAL REACTTION MECHANISM OF FLAVIN DEHYDROGENATION
Summary for 1C0L
| Entry DOI | 10.2210/pdb1c0l/pdb |
| Related | 1C0I 1C0K 1C0P |
| Descriptor | D-AMINO ACID OXIDASE, TRIFLUOROALANINE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | flavin containing protein alpha-beta-alpha motif, oxidoreductase |
| Biological source | Rhodosporidium toruloides |
| Total number of polymer chains | 1 |
| Total formula weight | 40543.54 |
| Authors | Umhau, S.,Molla, G.,Diederichs, K.,Pilone, M.S.,Ghisla, S.,Welte, W. (deposition date: 1999-07-16, release date: 2000-11-22, Last modification date: 2024-02-07) |
| Primary citation | Umhau, S.,Pollegioni, L.,Molla, G.,Diederichs, K.,Welte, W.,Pilone, M.S.,Ghisla, S. The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation. Proc.Natl.Acad.Sci.USA, 97:12463-12468, 2000 Cited by PubMed: 11070076DOI: 10.1073/pnas.97.23.12463 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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