1h7x Summary

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DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, TERNARY COMPLEX OF A MUTANT ENZYME (C671A), NADPH AND 5-FLUOROURACIL

The structure was published by Dobritzsch, D., Schneider, G., Schnackerz, K.D., and Lindqvist, Y., in 2001 in a paper entitled "Crystal Structure of Dihydropyrimidine Dehydrogenase, a Major Determinant of the Pharmacokinetics of the Anti-Cancer Drug 5-Fluorouracil" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2001.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of DIHYDROPYRIMIDINE DEHYDROGENASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A DIHYDROPYRIMIDINE DEHYDROGENASE Q28943 (1-1025) (DPYD_PIG)search Sus scrofasearch 100% 1025 99%
B DIHYDROPYRIMIDINE DEHYDROGENASE Q28943 (1-1025) (DPYD_PIG)search Sus scrofasearch 100% 1025 99%
C DIHYDROPYRIMIDINE DEHYDROGENASE Q28943 (1-1025) (DPYD_PIG)search Sus scrofasearch 100% 1025 99%
D DIHYDROPYRIMIDINE DEHYDROGENASE Q28943 (1-1025) (DPYD_PIG)search Sus scrofasearch 100% 1025 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q28943 (1 - 1025) DIHYDROPYRIMIDINE DEHYDROGENASE Sus scrofa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (Q28943) Dihydropyrimidine dehydrogenase, N-terminal domainsearch, FMN-linked oxidoreductasessearch, C-terminal domain of adrenodoxin reductase-likesearch, N-terminal domain of adrenodoxin reductase-likesearch, Ferredoxin domains from multidomain proteinssearch Alpha-Beta Plaitssearch, Fumarate Reductase Iron-sulfur Protein; Chain B, domain 2search, FAD/NAD(P)-binding domainsearch, Aldolase class Isearch PF01180: Dihydroorotate dehydrogenasesearch, PF13450: NAD(P)-binding Rossmann-like domainsearch, PF14691: Dihydroprymidine dehydrogenase domain II, 4Fe-4S clustersearch, PF14697: 4Fe-4S dicluster domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B, C, D (Q28943) dihydroorotate dehydrogenase activitysearch oxidoreductase activitysearch 4 iron, 4 sulfur cluster bindingsearch iron-sulfur cluster bindingsearch catalytic activitysearch oxidoreductase activity, acting on the CH-CH group of donorssearch protein homodimerization activitysearch dihydropyrimidine dehydrogenase (NADP+) activitysearch FMN bindingsearch NADP bindingsearch flavin adenine dinucleotide bindingsearch nucleotide bindingsearch metal ion bindingsearch cytoplasmsearch oxidation-reduction processsearch UMP biosynthetic processsearch uracil catabolic processsearch thymidine catabolic processsearch beta-alanine biosynthetic processsearch

Chain InterPro annotation
A, B, C, D Dihydroorotate dehydrogenase domainsearch Alpha-helical ferredoxinsearch Dihydroorotate dehydrogenase, class 1/ 2search Aldolase-type TIM barrelsearch 4Fe-4S ferredoxin-type, iron-sulphur binding domainsearch 4Fe-4S ferredoxin, iron-sulphur binding, conserved sitesearch Dihydroprymidine dehydrogenase domain IIsearch