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5BOO

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM265

Functional Information from GO Data
ChainGOidnamespacecontents
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0016020cellular_componentmembrane
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0016020cellular_componentmembrane
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue D65 A 1001
ChainResidue
ALEU172
AILE263
AARG265
AILE272
ALEU531
AVAL532
AMET536
AGLY181
AGLU182
ACYS184
AHIS185
APHE188
ALEU197
APHE227
ALEU240

site_idAC2
Number of Residues17
Detailsbinding site for residue FMN A 1002
ChainResidue
AALA224
AALA225
AGLY226
ALYS229
ATHR249
AASN274
ALYS429
ASER457
AASN458
ASER477
AGLY478
ASER505
AGLY506
AGLY507
ATYR528
ASER529
AORO1003

site_idAC3
Number of Residues12
Detailsbinding site for residue ORO A 1003
ChainResidue
ALYS229
AASN274
ACYS276
AGLY277
APHE278
AASN342
ASER344
ASER345
AASN347
AASN458
ATHR459
AFMN1002

site_idAC4
Number of Residues14
Detailsbinding site for residue D65 B 1001
ChainResidue
BLEU172
BGLY181
BGLU182
BCYS184
BHIS185
BPHE188
BLEU197
BPHE227
BLEU240
BILE263
BARG265
BILE272
BLEU531
BMET536

site_idAC5
Number of Residues17
Detailsbinding site for residue FMN B 1002
ChainResidue
BALA224
BALA225
BGLY226
BLYS229
BTHR249
BASN274
BLYS429
BSER457
BASN458
BSER477
BGLY478
BSER505
BGLY506
BGLY507
BTYR528
BSER529
BORO1003

site_idAC6
Number of Residues11
Detailsbinding site for residue ORO B 1003
ChainResidue
BLYS229
BASN274
BCYS276
BGLY277
BPHE278
BASN342
BSER345
BASN347
BASN458
BTHR459
BFMN1002

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. SfieiGTITprgQtGNakPR
ChainResidueDetails
ASER243-ARG262

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIAsGGIfSgldAleKIeAGA
ChainResidueDetails
AILE502-ALA522

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 Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16510978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20702404","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

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PDB entries from 2025-10-15

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