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7S87

Crystal Structure of Dihydroorotate dehydrogenase from Plasmodium falciparum in complex with Orotate, FMN, and inhibitor NCGC00600348-01

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 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
AILE472-ALA492

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ASER345
BSER345

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:16510978, ECO:0000269|PubMed:20702404
ChainResidueDetails
AALA225
BGLY477
BGLY505
BLEU528
ATHR249
ATHR429
AGLY477
AGLY505
ALEU528
BALA225
BTHR249
BTHR429

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ALYS229
BPHE458
AASN274
AASN342
AASN347
APHE458
BLYS229
BASN274
BASN342
BASN347

224572

PDB entries from 2024-09-04

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