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1ddo
From Proteopedia
(New page: 200px<br /> <applet load="1ddo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddo, resolution 3.1Å" /> '''REDUCED D-AMINO ACID...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1DDO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with FAD, ITR and DTR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DDO OCA]]. | + | 1DDO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]] with FAD, ITR and DTR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3]]. Structure known Active Sites: FAA, FAB, FAC, FAD, FAE, FAF, FAG and FAH. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DDO OCA]]. |
==Reference== | ==Reference== | ||
Active site plasticity in D-amino acid oxidase: a crystallographic analysis., Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A, Biochemistry. 1997 May 13;36(19):5853-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9153426 9153426] | Active site plasticity in D-amino acid oxidase: a crystallographic analysis., Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A, Biochemistry. 1997 May 13;36(19):5853-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9153426 9153426] | ||
| + | [[Category: D-amino-acid oxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:17:09 2007'' |
Revision as of 11:12, 30 October 2007
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REDUCED D-AMINO ACID OXIDASE FROM PIG KIDNEY IN COMPLEX WITH IMINO-TRP
Overview
D-Amino acid oxidase (DAAO) is the prototype of the flavin-containing, oxidases. It catalyzes the oxidative deamination of various D-amino acids, ranging from D-Ala to D-Trp. We have carried out the X-ray analysis of, reduced DAAO in complex with the reaction product imino tryptophan (iTrp), and of the covalent adduct generated by the photoinduced reaction of the, flavin with 3-methyl-2-oxobutyric acid (kVal). These structures were, solved by combination of 8-fold density averaging and least-squares, refinement techniques. The FAD redox state of DAAO crystals was assessed, by single-crystal polarized absorption microspectrophotometry. iTrp binds, to the reduced enzyme with the N, C alpha, C, and C beta atoms positioned, 3.8 A from the re side of the flavin. The indole side chain points ... [(full description)]
About this Structure
1DDO is a [Single protein] structure of sequence from [Sus scrofa] with FAD, ITR and DTR as [ligands]. Active as [D-amino-acid oxidase], with EC number [1.4.3.3]. Structure known Active Sites: FAA, FAB, FAC, FAD, FAE, FAF, FAG and FAH. Full crystallographic information is available from [OCA].
Reference
Active site plasticity in D-amino acid oxidase: a crystallographic analysis., Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A, Biochemistry. 1997 May 13;36(19):5853-60. PMID:9153426
Page seeded by OCA on Tue Oct 30 13:17:09 2007
Categories: D-amino-acid oxidase | Single protein | Sus scrofa | Mattevi, A. | Todone, F. | DTR | FAD | ITR | Fad cofactor | Flavoenzyme | Oxidoreductase
