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5XFV

Crystal structures of FMN-bound form of dihydroorotate dehydrogenase from Trypanosoma brucei

Functional Information from GO Data
ChainGOidnamespacecontents
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006106biological_processfumarate metabolic process
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0020015cellular_componentglycosome
A0044205biological_process'de novo' UMP biosynthetic process
A0097014cellular_componentciliary plasm
A1990663molecular_functiondihydroorotate dehydrogenase (fumarate) activity
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006106biological_processfumarate metabolic process
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006222biological_processUMP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0020015cellular_componentglycosome
B0044205biological_process'de novo' UMP biosynthetic process
B0097014cellular_componentciliary plasm
B1990663molecular_functiondihydroorotate dehydrogenase (fumarate) activity
C0004152molecular_functiondihydroorotate dehydrogenase activity
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0006106biological_processfumarate metabolic process
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006222biological_processUMP biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0020015cellular_componentglycosome
C0044205biological_process'de novo' UMP biosynthetic process
C0097014cellular_componentciliary plasm
C1990663molecular_functiondihydroorotate dehydrogenase (fumarate) activity
D0004152molecular_functiondihydroorotate dehydrogenase activity
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0006106biological_processfumarate metabolic process
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0006222biological_processUMP biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0020015cellular_componentglycosome
D0044205biological_process'de novo' UMP biosynthetic process
D0097014cellular_componentciliary plasm
D1990663molecular_functiondihydroorotate dehydrogenase (fumarate) activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue FMN A 401
ChainResidue
AALA19
AASN195
ASER196
AGLY223
AVAL226
ACYS249
AGLY250
AGLY251
AGLY272
ATHR273
AMLI402
AALA20
AHOH502
AHOH505
AHOH539
AHOH596
AGLY21
ALYS44
ASER45
AASN68
AASN128
ALYS165
AVAL194

site_idAC2
Number of Residues12
Detailsbinding site for residue MLI A 402
ChainResidue
ALYS44
AASN68
AMET70
AGLY71
ALEU72
ACYS131
APRO132
AASN133
AASN195
AFMN401
AHOH513
AHOH530

site_idAC3
Number of Residues7
Detailsbinding site for residue MLI A 403
ChainResidue
AILE172
AARG239
AARG240
AHOH625
AHOH637
BLYS215
BGLN216

site_idAC4
Number of Residues4
Detailsbinding site for residue MLI A 404
ChainResidue
AARG51
ATHR52
AGLY53
AHOH562

site_idAC5
Number of Residues23
Detailsbinding site for residue FMN B 401
ChainResidue
BALA19
BALA20
BGLY21
BLYS44
BSER45
BASN68
BASN128
BLYS165
BVAL194
BASN195
BSER196
BGLY223
BVAL226
BCYS249
BGLY250
BGLY251
BGLY272
BTHR273
BMLI402
BHOH507
BHOH519
BHOH550
BHOH554

site_idAC6
Number of Residues12
Detailsbinding site for residue MLI B 402
ChainResidue
BLYS44
BASN68
BMET70
BGLY71
BLEU72
BCYS131
BPRO132
BASN133
BASN195
BFMN401
BHOH521
BHOH567

site_idAC7
Number of Residues8
Detailsbinding site for residue MLI B 403
ChainResidue
ALYS215
AGLN216
APHE218
BILE172
BARG239
BARG240
BHOH611
BHOH670

site_idAC8
Number of Residues6
Detailsbinding site for residue MLI B 404
ChainResidue
BARG51
BTHR52
BGLY53
BHOH552
BHOH625
CTHR26

site_idAC9
Number of Residues23
Detailsbinding site for residue FMN C 401
ChainResidue
CSER45
CASN68
CASN128
CLYS165
CVAL194
CASN195
CSER196
CGLY223
CVAL226
CCYS249
CGLY250
CGLY251
CGLY272
CTHR273
CMLI402
CHOH506
CHOH508
CHOH543
CHOH565
CALA19
CALA20
CGLY21
CLYS44

site_idAD1
Number of Residues12
Detailsbinding site for residue MLI C 402
ChainResidue
CLYS44
CASN68
CMET70
CGLY71
CLEU72
CCYS131
CPRO132
CASN133
CASN195
CFMN401
CHOH511
CHOH527

site_idAD2
Number of Residues5
Detailsbinding site for residue MLI C 403
ChainResidue
CILE172
CARG239
CARG240
DLYS215
DGLN216

site_idAD3
Number of Residues4
Detailsbinding site for residue MLI C 404
ChainResidue
CARG51
CTHR52
CGLY53
CHOH545

site_idAD4
Number of Residues7
Detailsbinding site for residue MLI C 405
ChainResidue
CLYS215
CGLN216
CHOH542
CHOH604
DILE172
DARG239
DARG240

site_idAD5
Number of Residues24
Detailsbinding site for residue FMN D 401
ChainResidue
DALA19
DALA20
DGLY21
DLYS44
DSER45
DASN68
DASN128
DLYS165
DVAL194
DASN195
DSER196
DGLY223
DVAL226
DCYS249
DGLY250
DGLY251
DGLY272
DTHR273
DMLI402
DHOH501
DHOH503
DHOH505
DHOH520
DHOH541

site_idAD6
Number of Residues11
Detailsbinding site for residue MLI D 402
ChainResidue
DLYS44
DMET70
DGLY71
DLEU72
DCYS131
DPRO132
DASN133
DASN195
DFMN401
DHOH505
DHOH506

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18312275","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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