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1UUM

Rat dihydroorotate dehydrogenase (DHOD)in complex with atovaquone

Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006225biological_processUDP biosynthetic process
A0007565biological_processfemale pregnancy
A0007595biological_processlactation
A0009220biological_processpyrimidine ribonucleotide biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0031000biological_processresponse to caffeine
A0042594biological_processresponse to starvation
A0043025cellular_componentneuronal cell body
A0043065biological_processpositive regulation of apoptotic process
A0044205biological_process'de novo' UMP biosynthetic process
A0048038molecular_functionquinone binding
A0048039molecular_functionubiquinone binding
A0072528biological_processpyrimidine-containing compound biosynthetic process
A0090140biological_processregulation of mitochondrial fission
A0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
A1903576biological_processresponse to L-arginine
B0004151molecular_functiondihydroorotase activity
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006225biological_processUDP biosynthetic process
B0007565biological_processfemale pregnancy
B0007595biological_processlactation
B0009220biological_processpyrimidine ribonucleotide biosynthetic process
B0009410biological_processresponse to xenobiotic stimulus
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0031000biological_processresponse to caffeine
B0042594biological_processresponse to starvation
B0043025cellular_componentneuronal cell body
B0043065biological_processpositive regulation of apoptotic process
B0044205biological_process'de novo' UMP biosynthetic process
B0048038molecular_functionquinone binding
B0048039molecular_functionubiquinone binding
B0072528biological_processpyrimidine-containing compound biosynthetic process
B0090140biological_processregulation of mitochondrial fission
B0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
B1903576biological_processresponse to L-arginine
Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfvevGSVTpqpQeGNprPR
ChainResidueDetails
AGLY114-ARG133

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIqAGA
ChainResidueDetails
AILE330-ALA350

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15044733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ASER215
APHE149
ALYS255

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
BSER215
BPHE149
BLYS255

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ASER215

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
BSER215

246704

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