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3I68

Plasmodium falciparum dihydroorotate dehydrogenase bound with triazolopyrimidine-based inhibitor DSM2

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 Residues13
DetailsBINDING SITE FOR RESIDUE J4Z A 1001
ChainResidue
ALEU172
ALEU240
AARG265
ALEU531
AVAL532
AGLY181
ACYS184
AHIS185
APHE188
ALEU197
APHE227
ACYS233
AILE237

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN A 1002
ChainResidue
AHOH2
AHOH16
AALA224
AALA225
AGLY226
ALYS229
ATHR249
AASN274
AASN342
ALYS429
ASER457
AASN458
ASER477
AGLY478
ALEU481
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
ATHR459
AGLY507
AGLY535
ALEU558

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALYS229
AASN274
AASN342
AASN347
APHE488

218853

PDB entries from 2024-04-24

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