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7KYV

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM634 (3-methyl-N-(1-(5-methylisoxazol-3-yl)ethyl)-4-(4-(trifluoromethyl)benzyl)-1H-pyrrole-2-carboxamide)

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 Residues14
Detailsbinding site for residue XBY A 1001
ChainResidue
ATYR168
ALEU191
AILE263
AARG265
AVAL532
AMET536
APHE171
ALEU172
AGLY181
AGLU182
ACYS184
AHIS185
ALEU187
APHE188

site_idAC2
Number of Residues23
Detailsbinding site for residue FMN A 1002
ChainResidue
AALA224
AALA225
AGLY226
ALYS229
ATHR249
AASN274
AASN342
ALYS429
ASER457
AASN458
ATHR459
ASER477
AGLY478
ALEU481
ASER505
AGLY506
AGLY507
ATYR528
ASER529
AORO1003
AHOH1114
AHOH1119
AHOH1134

site_idAC3
Number of Residues12
Detailsbinding site for residue ORO A 1003
ChainResidue
ALYS229
AASN274
ACYS276
AGLY277
APHE278
AASN342
ASER345
APRO346
AASN347
AASN458
ATHR459
AFMN1002

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 1004
ChainResidue
AASN258
AALA259

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 1005
ChainResidue
AGLU164
APHE165
APRO198
ATYR199

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 1006
ChainResidue
ALYS193
AGLY231
AVAL232
AASN289
AARG296
AHOH1125

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 1007
ChainResidue
AASP180
AGLY181
AILE263
APHE264
AARG265
AASN381

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

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PDB entries from 2024-07-24

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