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-Structure paper
| Title | The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. |
|---|---|
| Journal, issue, pages | EMBO J., Vol. 19, Page 4204-4215, Year 2000 |
| Publish date | Jul 4, 2000 (structure data deposition date) |
Authors | Pawelek, P.D. / Cheah, J. / Coulombe, R. / Macheroux, P. / Ghisla, S. / Vrielink, A. |
External links | EMBO J. / PubMed:10944103 |
| Methods | X-ray diffraction |
| Resolution | 2 Å |
| Structure data | ![]() PDB-1f8r: ![]() PDB-1f8s: |
| Chemicals | ![]() ChemComp-NAG: ![]() ChemComp-CIT: ![]() ChemComp-FAD: ![]() ChemComp-HOH: ![]() ChemComp-BE2: |
| Source |
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Keywords | OXIDOREDUCTASE / FLAVOENZYME / OXIDASE / ENANTIOMERIC SPECIFICITY / ACTIVE SITE FUNNEL / HELICAL DOMAIN / FAD-BINDING DOMAIN / o-AMINOBENZOATE |
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calloselasma rhodostoma (Malayan pit viper)
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