7LJS
Porcine Dihydropyrimidine dehydrogenase (DPD) complexed with 5-Ethynyluracil (5EU) - Open Form
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
B | SCOP2B Superfamily | FMN-linked oxidoreductases | 8001523 | 3000014 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Thioredoxin reductase-like | 8017506 | 3000050 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | 4Fe-4S ferredoxins | 8001525 | 3000020 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | alpha-helical ferredoxin | 8001521 | 3000026 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | 4Fe-4S ferredoxins | 8001525 | 3000020 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | FMN-linked oxidoreductases | 8001523 | 3000014 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Thioredoxin reductase-like | 8017506 | 3000050 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | alpha-helical ferredoxin | 8001521 | 3000026 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | alpha-helical ferredoxin | 8001521 | 3000026 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | 4Fe-4S ferredoxins | 8001525 | 3000020 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | FMN-linked oxidoreductases | 8001523 | 3000014 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Thioredoxin reductase-like | 8017506 | 3000050 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Thioredoxin reductase-like | 8017506 | 3000050 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | FMN-linked oxidoreductases | 8001523 | 3000014 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | alpha-helical ferredoxin | 8001521 | 3000026 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | 4Fe-4S ferredoxins | 8001525 | 3000020 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B | Fer4_20 | e7ljsB2 | A: alpha arrays | X: alpha-helical ferredoxin-like | H: alpha-helical ferredoxin (From Topology) | T: alpha-helical ferredoxin | F: Fer4_20 | ECOD (1.6) |
B | Fer4_21 | e7ljsB3 | A: a+b two layers | X: 4Fe-4S ferredoxin (From Topology) | H: 4Fe-4S ferredoxin (From Topology) | T: 4Fe-4S ferredoxin | F: Fer4_21 | ECOD (1.6) |
B | DHO_dh | e7ljsB1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHO_dh | ECOD (1.6) |
B | Pyr_redox_2_3 | e7ljsB4 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: Pyr_redox_2_3 | ECOD (1.6) |
B | Pyr_redox_2 | e7ljsB5 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: Nucleotide-binding domain | F: Pyr_redox_2 | ECOD (1.6) |
C | Fer4_20 | e7ljsC3 | A: alpha arrays | X: alpha-helical ferredoxin-like | H: alpha-helical ferredoxin (From Topology) | T: alpha-helical ferredoxin | F: Fer4_20 | ECOD (1.6) |
C | Fer4_21 | e7ljsC2 | A: a+b two layers | X: 4Fe-4S ferredoxin (From Topology) | H: 4Fe-4S ferredoxin (From Topology) | T: 4Fe-4S ferredoxin | F: Fer4_21 | ECOD (1.6) |
C | DHO_dh | e7ljsC4 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHO_dh | ECOD (1.6) |
C | Pyr_redox_2_3 | e7ljsC1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: Pyr_redox_2_3 | ECOD (1.6) |
C | Pyr_redox_2 | e7ljsC5 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: Nucleotide-binding domain | F: Pyr_redox_2 | ECOD (1.6) |
D | Fer4_20 | e7ljsD5 | A: alpha arrays | X: alpha-helical ferredoxin-like | H: alpha-helical ferredoxin (From Topology) | T: alpha-helical ferredoxin | F: Fer4_20 | ECOD (1.6) |
D | Fer4_21 | e7ljsD3 | A: a+b two layers | X: 4Fe-4S ferredoxin (From Topology) | H: 4Fe-4S ferredoxin (From Topology) | T: 4Fe-4S ferredoxin | F: Fer4_21 | ECOD (1.6) |
D | DHO_dh | e7ljsD2 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHO_dh | ECOD (1.6) |
D | Pyr_redox_2_3 | e7ljsD1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: Pyr_redox_2_3 | ECOD (1.6) |
D | Pyr_redox_2 | e7ljsD4 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: Nucleotide-binding domain | F: Pyr_redox_2 | ECOD (1.6) |
A | Fer4_20 | e7ljsA3 | A: alpha arrays | X: alpha-helical ferredoxin-like | H: alpha-helical ferredoxin (From Topology) | T: alpha-helical ferredoxin | F: Fer4_20 | ECOD (1.6) |
A | Fer4_21 | e7ljsA5 | A: a+b two layers | X: 4Fe-4S ferredoxin (From Topology) | H: 4Fe-4S ferredoxin (From Topology) | T: 4Fe-4S ferredoxin | F: Fer4_21 | ECOD (1.6) |
A | DHO_dh | e7ljsA2 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHO_dh | ECOD (1.6) |
A | Pyr_redox_2_3 | e7ljsA4 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: Pyr_redox_2_3 | ECOD (1.6) |
A | Pyr_redox_2 | e7ljsA1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: Nucleotide-binding domain | F: Pyr_redox_2 | ECOD (1.6) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF07992 | Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox_2) | Pyridine nucleotide-disulphide oxidoreductase | This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. | Domain | |
PF01180 | Dihydroorotate dehydrogenase (DHO_dh) | Dihydroorotate dehydrogenase | - | Domain | |
PF14691 | Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster (Fer4_20) | Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster | Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyses the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds [1]. This doma ... | Domain | |
PF14697 | 4Fe-4S dicluster domain (Fer4_21) | 4Fe-4S dicluster domain | Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contai ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR013785 | Aldolase-type TIM barrel | Homologous Superfamily | |
IPR005720 | Dihydroorotate dehydrogenase, catalytic | Domain | |
IPR036188 | FAD/NAD(P)-binding domain superfamily | Homologous Superfamily | |
IPR009051 | Alpha-helical ferredoxin | Homologous Superfamily | |
IPR017900 | 4Fe-4S ferredoxin, iron-sulphur binding, conserved site | Conserved Site | |
IPR028261 | Dihydroprymidine dehydrogenase domain II | Domain | |
IPR017896 | 4Fe-4S ferredoxin-type, iron-sulphur binding domain | Domain | |
IPR023753 | FAD/NAD(P)-binding domain | Domain |