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6VTN

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM557

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 Residues12
Detailsbinding site for residue RL7 A 1001
ChainResidue
ATYR168
AARG265
AVAL532
AGLY535
APHE171
ALEU172
ACYS175
AGLY181
AHIS185
ALEU187
ALEU191
AILE263

site_idAC2
Number of Residues23
Detailsbinding site for residue FMN A 1002
ChainResidue
AALA224
AALA225
AGLY226
ALYS229
ATHR249
AASN274
AASN342
ALYS429
ASER457
AASN458
ASER477
AGLY478
ALEU481
ASER505
AGLY506
AGLY507
ATYR528
ASER529
AORO1003
AHOH1103
AHOH1114
AHOH1125
AHOH1132

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
ATHR249
ATHR459
AGLY507
AGLY535
ALEU558
AALA225

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

219869

PDB entries from 2024-05-15

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