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3MJY

Crystal structure of dihydroorotate dehydrogenase from Leishmania major in complex with 5-Aminoorotic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006106biological_processfumarate metabolic process
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
A0097014cellular_componentciliary plasm
A1990663molecular_functiondihydroorotate dehydrogenase (fumarate) activity
B0000166molecular_functionnucleotide binding
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006106biological_processfumarate metabolic process
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006222biological_processUMP biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0044205biological_process'de novo' UMP biosynthetic process
B0097014cellular_componentciliary plasm
B1990663molecular_functiondihydroorotate dehydrogenase (fumarate) activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FMN A 313
ChainResidue
AALA19
ALYS165
AILE194
AASN195
AGLY222
AGLY223
AVAL226
ACYS249
AGLY250
AGLY251
AGLY272
AALA20
ATHR273
AIJZ314
AHOH337
AHOH341
AHOH393
AHOH470
AGLY21
ALYS44
ASER45
ATYR59
AASN68
AMET70
AASN128

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE IJZ A 314
ChainResidue
ALYS44
AASN68
AMET70
AGLY71
ALEU72
AASN128
AASN195
ASER196
AFMN313

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN B 313
ChainResidue
BALA19
BALA20
BGLY21
BLYS44
BSER45
BTYR59
BASN68
BMET70
BASN128
BLYS165
BILE194
BASN195
BGLY222
BGLY223
BVAL226
BCYS249
BGLY250
BGLY251
BGLY272
BTHR273
BIJZ314
BHOH348
BHOH379
BHOH434

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IJZ B 314
ChainResidue
BLYS44
BASN68
BMET70
BGLY71
BLEU72
BASN128
BASN195
BSER196
BFMN313
BHOH363
BHOH457

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 315
ChainResidue
ALEU231
BVAL202
BILE203
BHOH444
BHOH534

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 315
ChainResidue
AVAL202
AILE203
AHOH438
AHOH492
BLEU231
BLEU260

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 316
ChainResidue
AASP171
APHE172
AALA173
BASN199
BLYS215

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 316
ChainResidue
AASN199
ALYS215
BASP171
BPHE172
BHOH400

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 317
ChainResidue
AGLU206
ATHR207
AGLU208
BGLU206
BTHR207
BGLU208
BARG310
BHOH487
BHOH522

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 318
ChainResidue
AHIS160
ASER161
AHOH536
AHOH537

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PDB entries from 2025-12-31

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