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6VND

Quaternary Complex of human dihydroorotate dehydrogenase (DHODH) with flavin mononucleotide (FMN), orotic acid and AG-636

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 Residues17
Detailsbinding site for residue R4P A 401
ChainResidue
ATYR37
ALEU66
ALEU67
AARG135
ATYR355
ATHR359
APRO363
ADDQ404
AHOH573
ALEU41
AMET42
AGLN46
APRO51
AALA54
AHIS55
AALA58
ATHR62

site_idAC2
Number of Residues11
Detailsbinding site for residue DET A 402
ChainResidue
AARG56
ALYS99
AHIS100
APRO124
AGLN125
AGLU126
AASN149
ASER150
AHIS151
ANA407
AHOH613

site_idAC3
Number of Residues14
Detailsbinding site for residue DET A 403
ChainResidue
AGLU138
AASP139
AGLN140
APRO289
ALYS306
APRO307
AASP310
AGLN314
AARG317
AASP392
AHOH528
AHOH542
AHOH545
AHOH611

site_idAC4
Number of Residues5
Detailsbinding site for residue DDQ A 404
ChainResidue
ALEU57
APHE61
ALEU67
APRO68
AR4P401

site_idAC5
Number of Residues6
Detailsbinding site for residue DDQ A 405
ChainResidue
AGLN140
AARG346
ATRP361
AGLN380
APHE382
AALA391

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 406
ChainResidue
AARG297
ASER298
AHOH521

site_idAC7
Number of Residues3
Detailsbinding site for residue NA A 407
ChainResidue
AGLU52
AARG56
ADET402

site_idAC8
Number of Residues2
Detailsbinding site for residue NA A 408
ChainResidue
AARG161
AGLU265

site_idAC9
Number of Residues4
Detailsbinding site for residue NA A 409
ChainResidue
ALYS226
AARG230
ASER269
AGLU273

site_idAD1
Number of Residues26
Detailsbinding site for residue FMN A 410
ChainResidue
AALA94
AALA95
AGLY96
ALYS99
AGLY118
ASER119
AASN144
ATYR146
AASN180
AASN211
ALYS254
ATHR282
AASN283
ATHR284
ASER304
AGLY305
ALEU308
AVAL332
AGLY333
AGLY334
ALEU354
ATYR355
ATHR356
AORO411
AHOH514
AHOH539

site_idAD2
Number of Residues11
Detailsbinding site for residue ORO A 411
ChainResidue
AASN283
ATHR284
AFMN410
ALYS99
AASN144
ATYR146
AGLY147
APHE148
AASN211
ASER214
AASN216

site_idAD3
Number of Residues3
Detailsbinding site for residue ACT A 412
ChainResidue
ATHR260
AGLN262
AHOH634

site_idAD4
Number of Residues5
Detailsbinding site for residue ACT A 413
ChainResidue
AALA162
ALYS166
ALYS226
AGLU265
AASP266

site_idAD5
Number of Residues2
Detailsbinding site for residue ACT A 414
ChainResidue
AARG248
AHOH561

site_idAD6
Number of Residues4
Detailsbinding site for residue GOL A 415
ChainResidue
AASP105
ATYR108
AHOH546
AHOH633

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL A 416
ChainResidue
APRO129
AARG130
APRO131
AARG145
AGLN238

site_idAD8
Number of Residues8
Detailsbinding site for residue GOL A 417
ChainResidue
AGLN164
AGLN167
AALA168
ATHR171
ALEU204
AASP206
AHOH506
AHOH525

site_idAD9
Number of Residues4
Detailsbinding site for residue GOL A 418
ChainResidue
AARG56
ALEU57
AHOH568
AHOH640

site_idAE1
Number of Residues6
Detailsbinding site for residue GOL A 419
ChainResidue
ATYR320
AALA321
AHIS393
AHOH505
AHOH543
AHOH550

site_idAE2
Number of Residues2
Detailsbinding site for residue GOL A 420
ChainResidue
AGLY47
ALEU48

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GfveiGSVTpkpQeGNprPR
ChainResidueDetails
AGLY113-ARG132

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGVsSgqdAleKIrAGA
ChainResidueDetails
AILE329-ALA349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000250
ChainResidueDetails
ATHR31-ARG395

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER214

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:10673429, ECO:0000269|PubMed:16480261
ChainResidueDetails
AALA95
ASER119
AASN180
AASN211
ALYS254
ATHR282
AGLY305
AGLY334
ATYR355

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ALYS99
AASN144
AASN283

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 109
ChainResidueDetails
AASN144electrostatic stabiliser
APHE148activator, electrostatic stabiliser, enhance reactivity, polar/non-polar interaction
ASER214electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar/non-polar interaction, proton acceptor, proton donor, proton relay
AASN216electrostatic stabiliser
ATHR217activator, electrostatic stabiliser, enhance reactivity, hydrogen bond acceptor
ALYS254electrostatic stabiliser, hydrogen bond donor
AASN283electrostatic stabiliser

227344

PDB entries from 2024-11-13

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