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3SFK

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM267

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE D67 A 1001
ChainResidue
ALEU172
AILE263
AARG265
AILE272
ALEU531
AVAL532
AMET536
AGLY181
AGLU182
ACYS184
AHIS185
APHE188
ALEU197
APHE227
ALEU240

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 1002
ChainResidue
AHOH2
AALA224
AALA225
AGLY226
ALYS229
ATHR249
AASN274
AASN342
ALYS429
ASER457
AASN458
ASER477
AGLY478
ASER505
AGLY506
AGLY507
ATYR528
ASER529
AORO1003

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ORO A 1003
ChainResidue
ALYS229
AASN274
ACYS276
AGLY277
APHE278
AASN342
ASER345
AASN347
AASN458
ATHR459
AFMN1002

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 Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ASER345

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16510978, ECO:0000269|PubMed:20702404
ChainResidueDetails
AALA225
ATHR249
ALYS429
ASER477
ASER505
ATYR528

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS229
AASN274
AASN342
AASN347
AASN458

221716

PDB entries from 2024-06-26

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