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6QU7

Crystal structure of human DHODH in complex with BAY 2402234

Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005829cellular_componentcytosol
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006225biological_processUDP biosynthetic process
A0009220biological_processpyrimidine ribonucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0044205biological_process'de novo' UMP biosynthetic process
A0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ORO A 401
ChainResidue
ALYS100
ATHR285
AFMN402
AASN145
ATYR147
AGLY148
APHE149
AASN212
ASER215
AASN217
AASN284

site_idAC2
Number of Residues26
Detailsbinding site for residue FMN A 402
ChainResidue
AALA95
AALA96
AGLY97
ALYS100
AGLY119
ASER120
AASN145
ATYR147
AASN181
AASN212
ALYS255
ATHR283
AASN284
ATHR285
ASER305
AGLY306
ALEU309
AVAL333
AGLY334
AGLY335
ALEU355
ATYR356
ATHR357
AORO401
AHOH513
AHOH556

site_idAC3
Number of Residues20
Detailsbinding site for residue JJE A 403
ChainResidue
ATYR38
AMET43
ALEU46
AGLN47
ALEU50
APRO52
AALA55
AHIS56
ALEU58
AALA59
APHE62
ATHR63
ALEU67
ALEU68
APHE98
AARG136
ATYR356
ATHR360
APRO364
AHOH575

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 404
ChainResidue
AARG245
AVAL247
AHIS248

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG246
AARG249

site_idAC6
Number of Residues7
Detailsbinding site for residue ACT A 406
ChainResidue
ALYS307
APRO308
AASP311
ATHR314
AGLN315
AARG318
AHOH505

site_idAC7
Number of Residues5
Detailsbinding site for residue ACT A 407
ChainResidue
AALA169
ATHR172
ALEU205
AASP207
AHOH506

site_idAC8
Number of Residues2
Detailsbinding site for residue ACT A 408
ChainResidue
AARG57
AHIS152

site_idAC9
Number of Residues3
Detailsbinding site for residue ACT A 409
ChainResidue
ALYS167
ALYS227
AARG231

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfveiGSVTpkpQeGNprPR
ChainResidueDetails
AGLY114-ARG133

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA
ChainResidueDetails
AILE330-ALA350

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000250
ChainResidueDetails
ATHR32-ARG396

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER215

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261
ChainResidueDetails
AALA96
ASER120
AASN181
AASN212
ALYS255
ATHR283
AGLY306
AGLY335
ATYR356

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ALYS100
AASN145
AASN284

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 109
ChainResidueDetails
AASN145electrostatic stabiliser
APHE149activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction
ASER215electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay
AASN217electrostatic stabiliser
ATHR218activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor
ALYS255electrostatic stabiliser, hydrogen bond donor
AASN284electrostatic stabiliser

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PDB entries from 2024-11-20

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