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1F76

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP biosynthetic process
A0009220biological_processpyrimidine ribonucleotide biosynthetic process
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0044205biological_process'de novo' UMP biosynthetic process
A0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006222biological_processUMP biosynthetic process
B0009220biological_processpyrimidine ribonucleotide biosynthetic process
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0044205biological_process'de novo' UMP biosynthetic process
B0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
D0004152molecular_functiondihydroorotate dehydrogenase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0006222biological_processUMP biosynthetic process
D0009220biological_processpyrimidine ribonucleotide biosynthetic process
D0010181molecular_functionFMN binding
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0044205biological_process'de novo' UMP biosynthetic process
D0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
E0004152molecular_functiondihydroorotate dehydrogenase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
E0006221biological_processpyrimidine nucleotide biosynthetic process
E0006222biological_processUMP biosynthetic process
E0009220biological_processpyrimidine ribonucleotide biosynthetic process
E0010181molecular_functionFMN binding
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
E0044205biological_process'de novo' UMP biosynthetic process
E0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN A 1337
ChainResidue
AALA61
ATHR245
ATHR247
ASER267
AGLY268
ALEU271
AVAL295
AGLY296
AGLY297
ATYR318
ASER319
AALA62
AORO1338
AHOH1352
AHOH1404
AHOH1675
AGLY63
ALYS66
ATHR86
AASN111
AASN139
AASN172
ALYS217

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ORO A 1338
ChainResidue
ALYS66
AASN111
AMSE113
AGLY114
APHE115
AASN172
ASER175
AASN177
AASN246
ATHR247
AFMN1337

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ORO A 1339
ChainResidue
AMSE1
ALEU37
AVAL38
AARG39
AGLN40
APRO326
AHOH1517
AHOH1528
AHOH1677

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 1437
ChainResidue
BALA61
BALA62
BGLY63
BLYS66
BTHR86
BASN111
BASN139
BASN172
BLYS217
BTHR245
BASN246
BTHR247
BSER267
BGLY268
BVAL295
BGLY296
BGLY297
BTYR318
BSER319
BFMT1439
BFMT1440
BHOH1441
BHOH1463

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN D 1537
ChainResidue
DALA61
DALA62
DGLY63
DLYS66
DTHR86
DASN111
DASN139
DASN172
DLYS217
DTHR245
DASN246
DTHR247
DSER267
DGLY268
DVAL295
DGLY296
DGLY297
DTYR318
DSER319
DFMT1538
DFMT1539
DHOH1542
DHOH1561
DHOH1564

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ORO D 1540
ChainResidue
DMSE1
DLEU37
DVAL38
DGLN40
DPRO326
DHOH1617

site_idAC7
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FMN E 1637
ChainResidue
ELYS66
ETHR86
ELEU100
EASN111
EASN139
EASN172
ELYS217
ETHR245
EASN246
ETHR247
ESER267
EGLY268
ELEU271
EVAL295
EGLY296
EGLY297
ETYR318
ESER319
EFMT1638
EFMT1640
EHOH1641
EHOH1653
EHOH1693
EALA61
EALA62
EGLY63

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 1438
ChainResidue
BASN111
BASN177
BASN246
BTHR247
BFMT1439
BFMT1440

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 1439
ChainResidue
BPHE115
BASN172
BSER175
BASN246
BFMN1437
BFMT1438
BFMT1440

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT B 1440
ChainResidue
BLYS66
BMSE113
BGLY114
BPHE115
BSER175
BASN177
BFMN1437
BFMT1438
BFMT1439

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT D 1538
ChainResidue
DASN172
DSER175
DASN246
DFMN1537
DFMT1539

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT D 1539
ChainResidue
DLYS66
DMSE113
DGLY114
DPHE115
DSER175
DASN177
DFMN1537
DFMT1538
DHOH1557

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT E 1638
ChainResidue
ELYS66
EMSE113
EGLY114
EPHE115
EASN177
EFMN1637
EFMT1639
EFMT1640

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT E 1639
ChainResidue
EASN111
EASN177
ETHR247
EGLY265
EFMT1638
EFMT1640

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT E 1640
ChainResidue
EASN172
ESER175
EPRO176
EASN246
EFMN1637
EFMT1638
EFMT1639

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GsieiGTVTprpQpGNdkPR
ChainResidueDetails
AGLY80-ARG99

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGIdSviaAreKIaAGA
ChainResidueDetails
AILE292-ALA312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12220493","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ASER175
ATHR178
APHE115
ALYS217

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
BSER175
BTHR178
BPHE115
BLYS217

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
DSER175
DTHR178
DPHE115
DLYS217

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ESER175
ETHR178
EPHE115
ELYS217

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ASER175

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
BSER175

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
DSER175

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ESER175

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PDB entries from 2025-10-08

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