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1h7w
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1H7W 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 SF4, FMN and FAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1H7W 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 SF4, FMN and FAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Dihydropyrimidine_dehydrogenase_(NADP(+)) Dihydropyrimidine dehydrogenase (NADP(+))]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.2 1.3.1.2]]. Structure known Active Sites: AC5, AC6, BC5, BC6, CC5, CC6, DC5 and DC6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H7W OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil., Dobritzsch D, Schneider G, Schnackerz KD, Lindqvist Y, EMBO J. 2001 Feb 15;20(4):650-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11179210 11179210] | Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil., Dobritzsch D, Schneider G, Schnackerz KD, Lindqvist Y, EMBO J. 2001 Feb 15;20(4):650-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11179210 11179210] | ||
| + | [[Category: Dihydropyrimidine dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: pyrimidine catabolism]] | [[Category: pyrimidine catabolism]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:29:17 2007'' |
Revision as of 08:24, 30 October 2007
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DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG
Overview
Dihydropyrimidine dehydrogenase catalyzes the first step in pyrimidine, degradation: the NADPH-dependent reduction of uracil and thymine to the, corresponding 5,6-dihydropyrimidines. Its controlled inhibition has become, an adjunct target for cancer therapy, since the enzyme is also responsible, for the rapid breakdown of the chemotherapeutic drug 5-fluorouracil. The, crystal structure of the homodimeric pig liver enzyme (2x 111 kDa), determined at 1.9 A resolution reveals a highly modular subunit, organization, consisting of five domains with different folds., Dihydropyrimidine dehydrogenase contains two FAD, two FMN and eight, [4Fe-4S] clusters, arranged in two electron transfer chains that pass the, dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved, ... [(full description)]
About this Structure
1H7W is a [Single protein] structure of sequence from [Sus scrofa] with SF4, FMN and FAD as [ligands]. Active as [Dihydropyrimidine dehydrogenase (NADP(+))], with EC number [1.3.1.2]. Structure known Active Sites: AC5, AC6, BC5, BC6, CC5, CC6, DC5 and DC6. Full crystallographic information is available from [OCA].
Reference
Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil., Dobritzsch D, Schneider G, Schnackerz KD, Lindqvist Y, EMBO J. 2001 Feb 15;20(4):650-60. PMID:11179210
Page seeded by OCA on Tue Oct 30 10:29:17 2007
