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4XQ6

CRYSTAL STRUCTURE OF DIHYDROOROTATE DEHYDROGENSE from MYCOBACTERIUM TUBERCULOSIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP 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
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006222biological_processUMP biosynthetic process
B0009220biological_processpyrimidine ribonucleotide biosynthetic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0044205biological_process'de novo' UMP biosynthetic process
B0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue FMN A 401
ChainResidue
AALA65
ATHR240
AASN241
ASER263
AGLY264
ALEU267
AVAL291
AGLY292
AGLY293
AGLY313
ATYR314
AALA66
ATHR315
AHOH536
AHOH570
AHOH603
AGLY67
ATHR90
AASN115
AASN143
AASN176
ASER179
ALYS212

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 402
ChainResidue
APHE119
ATHR182
AHOH573

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 403
ChainResidue
AASN115
ATHR242
AGLY261
AHOH601

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 401
ChainResidue
AHIS94
AHOH513
AHOH521
BASP227
BHOH506
BHOH528

site_idAC5
Number of Residues23
Detailsbinding site for residue FMN B 402
ChainResidue
BALA65
BALA66
BGLY67
BTHR90
BASN115
BASN143
BASN176
BLYS212
BTHR240
BASN241
BSER263
BGLY264
BLEU267
BVAL291
BGLY292
BGLY293
BGLY313
BTYR314
BTHR315
BHOH543
BHOH546
BHOH595
BHOH599

site_idAC6
Number of Residues5
Detailsbinding site for residue CL B 403
ChainResidue
BASN115
BPRO180
BTHR242
BHOH593
BHOH596

site_idAC7
Number of Residues2
Detailsbinding site for residue CL B 404
ChainResidue
BPHE119
BTHR182

site_idAC8
Number of Residues1
Detailsbinding site for residue CL B 405
ChainResidue
BARG133

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GyaeiGTVTahpQpGNpaPR
ChainResidueDetails
AGLY84-ARG103

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. LISvGGIeTaddAweRItAGA
ChainResidueDetails
ALEU288-ALA308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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