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Information on 1h7w
PDB: 1h7w
Compound: dihydropyrimidine dehydrogenase
Classification: ELECTRON TRANSFER
Entry date in PDB: 2001-02-23
Resolution [Å]: 1.90
R-Factor: 0.174


CHAIN: A
SWISS-PROT/TREMBL: Q28943
   KEYWORD: 3D-structure    4Fe-4S    FAD    Flavoprotein    FMN    Iron-sulfur    NADP    Oxidoreductase   
EC: 1.3.1.2
SCOP: a.1.2.2 All alpha proteins    Globin-like    alpha-helical ferredoxin    Dihydropyrimidine dehydrogenase, N-terminal domain    Dihydropyrimidine dehydrogenase, N-terminal domain    Pig (Sus scrofa)
SCOP: c.1.4.1 Alpha and beta proteins (a/b)    TIM beta/alpha-barrel    FMN-linked oxidoreductases    FMN-linked oxidoreductases    Dihydropyrimidine dehydrogenase, domain 4    Pig (Sus scrofa)
SCOP: c.3.1.1 Alpha and beta proteins (a/b)    FAD/NAD(P)-binding domain    FAD/NAD(P)-binding domain    C-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 3    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: d.58.1.5 Alpha and beta proteins (a+b)    Ferredoxin-like    4Fe-4S ferredoxins    Ferredoxin domains from multidomain proteins    Dihydropyrimidine dehydrogenase, C-terminal domain    Pig (Sus scrofa)
GO:  cytoplasm    membrane    dihydroorotate dehydrogenase activity    dihydroorotate oxidase activity    disulfide oxidoreductase activity    electron transporter activity    iron ion binding    oxidoreductase activity    'de novo' pyrimidine base biosynthesis    electron transport   


CHAIN: B
SWISS-PROT/TREMBL: Q28943
   KEYWORD: 3D-structure    4Fe-4S    FAD    Flavoprotein    FMN    Iron-sulfur    NADP    Oxidoreductase   
EC: 1.3.1.2
SCOP: a.1.2.2 All alpha proteins    Globin-like    alpha-helical ferredoxin    Dihydropyrimidine dehydrogenase, N-terminal domain    Dihydropyrimidine dehydrogenase, N-terminal domain    Pig (Sus scrofa)
SCOP: c.1.4.1 Alpha and beta proteins (a/b)    TIM beta/alpha-barrel    FMN-linked oxidoreductases    FMN-linked oxidoreductases    Dihydropyrimidine dehydrogenase, domain 4    Pig (Sus scrofa)
SCOP: c.3.1.1 Alpha and beta proteins (a/b)    FAD/NAD(P)-binding domain    FAD/NAD(P)-binding domain    C-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 3    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: d.58.1.5 Alpha and beta proteins (a+b)    Ferredoxin-like    4Fe-4S ferredoxins    Ferredoxin domains from multidomain proteins    Dihydropyrimidine dehydrogenase, C-terminal domain    Pig (Sus scrofa)
GO:  cytoplasm    membrane    dihydroorotate dehydrogenase activity    dihydroorotate oxidase activity    disulfide oxidoreductase activity    electron transporter activity    iron ion binding    oxidoreductase activity    'de novo' pyrimidine base biosynthesis    electron transport   


CHAIN: C
SWISS-PROT/TREMBL: Q28943
   KEYWORD: 3D-structure    4Fe-4S    FAD    Flavoprotein    FMN    Iron-sulfur    NADP    Oxidoreductase   
EC: 1.3.1.2
SCOP: a.1.2.2 All alpha proteins    Globin-like    alpha-helical ferredoxin    Dihydropyrimidine dehydrogenase, N-terminal domain    Dihydropyrimidine dehydrogenase, N-terminal domain    Pig (Sus scrofa)
SCOP: c.1.4.1 Alpha and beta proteins (a/b)    TIM beta/alpha-barrel    FMN-linked oxidoreductases    FMN-linked oxidoreductases    Dihydropyrimidine dehydrogenase, domain 4    Pig (Sus scrofa)
SCOP: c.3.1.1 Alpha and beta proteins (a/b)    FAD/NAD(P)-binding domain    FAD/NAD(P)-binding domain    C-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 3    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: d.58.1.5 Alpha and beta proteins (a+b)    Ferredoxin-like    4Fe-4S ferredoxins    Ferredoxin domains from multidomain proteins    Dihydropyrimidine dehydrogenase, C-terminal domain    Pig (Sus scrofa)
GO:  cytoplasm    membrane    dihydroorotate dehydrogenase activity    dihydroorotate oxidase activity    disulfide oxidoreductase activity    electron transporter activity    iron ion binding    oxidoreductase activity    'de novo' pyrimidine base biosynthesis    electron transport   


CHAIN: D
SWISS-PROT/TREMBL: Q28943
   KEYWORD: 3D-structure    4Fe-4S    FAD    Flavoprotein    FMN    Iron-sulfur    NADP    Oxidoreductase   
EC: 1.3.1.2
SCOP: a.1.2.2 All alpha proteins    Globin-like    alpha-helical ferredoxin    Dihydropyrimidine dehydrogenase, N-terminal domain    Dihydropyrimidine dehydrogenase, N-terminal domain    Pig (Sus scrofa)
SCOP: c.1.4.1 Alpha and beta proteins (a/b)    TIM beta/alpha-barrel    FMN-linked oxidoreductases    FMN-linked oxidoreductases    Dihydropyrimidine dehydrogenase, domain 4    Pig (Sus scrofa)
SCOP: c.3.1.1 Alpha and beta proteins (a/b)    FAD/NAD(P)-binding domain    FAD/NAD(P)-binding domain    C-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 3    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Dihydropyrimidine dehydrogenase, domain 2    Pig (Sus scrofa)
SCOP: d.58.1.5 Alpha and beta proteins (a+b)    Ferredoxin-like    4Fe-4S ferredoxins    Ferredoxin domains from multidomain proteins    Dihydropyrimidine dehydrogenase, C-terminal domain    Pig (Sus scrofa)
GO:  cytoplasm    membrane    dihydroorotate dehydrogenase activity    dihydroorotate oxidase activity    disulfide oxidoreductase activity    electron transporter activity    iron ion binding    oxidoreductase activity    'de novo' pyrimidine base biosynthesis    electron transport   
1h7w Image
Image Source: PDB

Stored Loops of 1h7w

Loops in ArchDB40 clusters

1h7w_A_238 - HE => SUBCLASS : 1.1.1
1h7w_A_374 - HE => SUBCLASS : 2.1.2
1h7w_A_238 - HE => SUBCLASS : 2.1.2
1h7w_A_238 - HE => SUBCLASS : 2.2.3
1h7w_A_557 - HE => SUBCLASS : 3.1.1
1h7w_A_799 - HE => SUBCLASS : 3.1.1
1h7w_A_268 - HE => SUBCLASS : 3.1.1
1h7w_A_647 - HE => SUBCLASS : 3.1.1
1h7w_A_342 - HE => SUBCLASS : 3.1.5
1h7w_A_717 - HE => SUBCLASS : 3.1.6
1h7w_A_557 - HE => SUBCLASS : 3.6.1
1h7w_A_647 - HE => SUBCLASS : 3.6.2
1h7w_A_618 - HE => SUBCLASS : 4.1.2
1h7w_A_771 - HE => SUBCLASS : 4.4.4
1h7w_A_197 - HE => SUBCLASS : 4.31.1
1h7w_A_859 - HA => SUBCLASS : 2.1.1
1h7w_A_535 - HA => SUBCLASS : 2.1.1
1h7w_A_391 - HA => SUBCLASS : 2.4.6
1h7w_A_971 - HA => SUBCLASS : 4.1.2
1h7w_A_402 - HA => SUBCLASS : 5.3.8
1h7w_A_402 - HA => SUBCLASS : 5.34.1
1h7w_A_971 - HA => SUBCLASS : 6.1.1
1h7w_A_812 - EH => SUBCLASS : 0.1.15
1h7w_A_334 - EH => SUBCLASS : 3.2.1
1h7w_A_190 - EH => SUBCLASS : 3.2.1
1h7w_A_636 - EH => SUBCLASS : 4.17.3
1h7w_A_636 - EH => SUBCLASS : 5.17.1
1h7w_A_944 - EH => SUBCLASS : 9.1.1
1h7w_A_386 - AR => SUBCLASS : 1.2.2
1h7w_A_540 - AR => SUBCLASS : 3.9.1
1h7w_A_433 - AR => SUBCLASS : 3.11.1
1h7w_A_109 - HH => SUBCLASS : 1.2.10
1h7w_A_97 - HH => SUBCLASS : 2.2.1

Loops in ArchDB95 clusters

1h7w_A_812 - EH => SUBCLASS : 0.1.7
1h7w_A_763 - EH => SUBCLASS : 1.2.12
1h7w_A_190 - EH => SUBCLASS : 3.5.1
1h7w_A_334 - EH => SUBCLASS : 3.5.1
1h7w_A_636 - EH => SUBCLASS : 4.15.1
1h7w_A_706 - EH => SUBCLASS : 4.37.1
1h7w_A_636 - EH => SUBCLASS : 5.23.1
1h7w_A_980 - EH => SUBCLASS : 8.29.1
1h7w_A_944 - EH => SUBCLASS : 9.1.1
1h7w_A_358 - EH => SUBCLASS : 10.9.1
1h7w_A_386 - AR => SUBCLASS : 1.1.5
1h7w_A_540 - AR => SUBCLASS : 3.4.1
1h7w_A_433 - AR => SUBCLASS : 3.15.1
1h7w_A_278 - AR => SUBCLASS : 5.74.1
1h7w_A_109 - HH => SUBCLASS : 1.2.5
1h7w_A_97 - HH => SUBCLASS : 2.2.1
1h7w_A_238 - HE => SUBCLASS : 1.1.1
1h7w_A_238 - HE => SUBCLASS : 1.1.2
1h7w_A_374 - HE => SUBCLASS : 2.1.4
1h7w_A_238 - HE => SUBCLASS : 2.1.4
1h7w_A_374 - HE => SUBCLASS : 2.5.1
1h7w_A_799 - HE => SUBCLASS : 3.1.1
1h7w_A_268 - HE => SUBCLASS : 3.1.1
1h7w_A_647 - HE => SUBCLASS : 3.1.1
1h7w_A_342 - HE => SUBCLASS : 3.1.1
1h7w_A_557 - HE => SUBCLASS : 3.1.1
1h7w_A_197 - HE => SUBCLASS : 3.1.3
1h7w_A_717 - HE => SUBCLASS : 3.3.5
1h7w_A_618 - HE => SUBCLASS : 3.4.2
1h7w_A_771 - HE => SUBCLASS : 4.9.5
1h7w_A_688 - HE => SUBCLASS : 4.37.1
1h7w_A_859 - HA => SUBCLASS : 2.1.1
1h7w_A_535 - HA => SUBCLASS : 2.1.1
1h7w_A_391 - HA => SUBCLASS : 2.5.3
1h7w_A_971 - HA => SUBCLASS : 4.1.1

Loops not clustered in ArchDB

1h7w_A_287 - AR
1h7w_A_419 - AR
1h7w_A_570 - AR
1h7w_A_731 - AR
1h7w_A_546 - EH
1h7w_A_607 - EH
1h7w_A_664 - EH
1h7w_A_790 - EH
1h7w_A_863 - EH
1h7w_A_476 - EH
1h7w_A_440 - EH
1h7w_A_303 - EH
1h7w_A_254 - EH
1h7w_A_214 - EH
1h7w_A_590 - HA
1h7w_A_738 - HA
1h7w_A_991 - HE
1h7w_A_958 - HE
1h7w_A_921 - HE
1h7w_A_826 - HE
1h7w_A_489 - HE
1h7w_A_445 - HE
1h7w_A_306 - HE
1h7w_A_152 - HE
1h7w_A_817 - HH
1h7w_A_226 - HH
1h7w_A_123 - HH
1h7w_A_86 - HH
1h7w_A_69 - HH
1h7w_A_31 - HH
1h7w_A_10 - HH
1h7w_A_880 - HH

Homologous structures to 1h7w classified in ArchDB

1gt8 A - percentage of sequence identity: 100
1gt8 B - percentage of sequence identity: 100
1gt8 C - percentage of sequence identity: 100
1gt8 D - percentage of sequence identity: 100
1gte A - percentage of sequence identity: 100
1gte B - percentage of sequence identity: 100
1gte C - percentage of sequence identity: 100
1gte D - percentage of sequence identity: 100
1gth A - percentage of sequence identity: 100
1gth B - percentage of sequence identity: 100
1gth C - percentage of sequence identity: 100
1gth D - percentage of sequence identity: 100
1h7w A - percentage of sequence identity: 100
1h7w B - percentage of sequence identity: 100
1h7w C - percentage of sequence identity: 100
1h7w D - percentage of sequence identity: 100
1h7x A - percentage of sequence identity: 99
1h7x B - percentage of sequence identity: 99
1h7x C - percentage of sequence identity: 99
1h7x D - percentage of sequence identity: 99