1h7w
From Proteopedia
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|PDB= 1h7w |SIZE=350|CAPTION= <scene name='initialview01'>1h7w</scene>, resolution 1.90Å | |PDB= 1h7w |SIZE=350|CAPTION= <scene name='initialview01'>1h7w</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC5:Fmn+Binding+Site+For+Chain+A'>AC5</scene>, <scene name='pdbsite=AC6:Fad+Binding+Site+For+Chain+A'>AC6</scene>, <scene name='pdbsite=BC5:Fmn+Binding+Site+For+Chain+B'>BC5</scene>, <scene name='pdbsite=BC6:Fad+Binding+Site+For+Chain+B'>BC6</scene>, <scene name='pdbsite=CC5:Fmn+Binding+Site+For+Chain+C'>CC5</scene>, <scene name='pdbsite=CC6:Fad+Binding+Site+For+Chain+C'>CC6</scene>, <scene name='pdbsite=DC5:Fmn+Binding+Site+For+Chain+D'>DC5</scene> and <scene name='pdbsite=DC6:Fad+Binding+Site+For+Chain+D'>DC6</scene> | |SITE= <scene name='pdbsite=AC5:Fmn+Binding+Site+For+Chain+A'>AC5</scene>, <scene name='pdbsite=AC6:Fad+Binding+Site+For+Chain+A'>AC6</scene>, <scene name='pdbsite=BC5:Fmn+Binding+Site+For+Chain+B'>BC5</scene>, <scene name='pdbsite=BC6:Fad+Binding+Site+For+Chain+B'>BC6</scene>, <scene name='pdbsite=CC5:Fmn+Binding+Site+For+Chain+C'>CC5</scene>, <scene name='pdbsite=CC6:Fad+Binding+Site+For+Chain+C'>CC6</scene>, <scene name='pdbsite=DC5:Fmn+Binding+Site+For+Chain+D'>DC5</scene> and <scene name='pdbsite=DC6:Fad+Binding+Site+For+Chain+D'>DC6</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= DPYD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | |GENE= DPYD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7w OCA], [http://www.ebi.ac.uk/pdbsum/1h7w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h7w RCSB]</span> | ||
}} | }} | ||
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[[Category: Schnackerz, K D.]] | [[Category: Schnackerz, K D.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: SF4]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
[[Category: flavin]] | [[Category: flavin]] | ||
| Line 36: | Line 36: | ||
[[Category: pyrimidine catabolism]] | [[Category: pyrimidine catabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:37 2008'' |
Revision as of 17:59, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | , , | ||||||
| Gene: | DPYD (Sus scrofa) | ||||||
| Activity: | Dihydropyrimidine dehydrogenase (NADP(+)), with EC number 1.3.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 coordination involving a glutamine residue. The ternary complex of an inactive mutant of the enzyme with bound NADPH and 5-fluorouracil reveals the architecture of the substrate-binding sites and residues responsible for recognition and binding of the drug.
About this Structure
1H7W is a Single protein structure of sequence from Sus scrofa. 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 Sun Mar 30 20:59:37 2008
