Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EP2

CRYSTAL STRUCTURE OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE B COMPLEXED WITH OROTATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0004589molecular_functiondihydroorotate dehydrogenase (NADH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0044205biological_process'de novo' UMP biosynthetic process
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0044205biological_process'de novo' UMP biosynthetic process
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 501
ChainResidue
AALA23
AILE196
AASN197
ATHR198
ASER221
AGLY222
AMET247
AGLY248
AGLY249
AGLY270
ATHR271
ASER24
AORO502
AHOH1003
AHOH1020
AGLY25
ALYS48
AALA49
AASN72
AASN104
AASN132
ALYS170

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ORO A 502
ChainResidue
ALYS48
AASN72
AILE74
AGLY75
ALEU76
AASN132
ACYS135
APRO136
AASN137
AASN197
ATHR198
AFMN501

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FAD B 503
ChainResidue
AGLU65
BLEU51
BARG53
BPRO54
BILE55
BSER56
BLEU70
BTYR71
BARG72
BTHR78
BGLY79
BTHR80
BILE120
BGLU221
BSER222
BARG223
BMET224
BHOH1006
BHOH1046
BHOH1050

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FES B 504
ChainResidue
BMET224
BALA225
BCYS226
BGLY227
BGLY229
BALA230
BCYS231
BTYR232
BCYS234
BCYS249

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GsimvKATTlhpRfGNptPR
ChainResidueDetails
AGLY43-ARG62

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGmGGVaNaqdVleMYmAGA
ChainResidueDetails
AILE244-ALA264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING:
ChainResidueDetails
BARG53
BLEU70
BGLY79
BCYS226
BCYS231
BCYS234
BCYS249

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING:
ChainResidueDetails
ASER24
AGLY248
AGLY270
ALYS48
AASN72
AASN104
AASN132
ALYS170
AILE196
AASN197
AGLY222

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon