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4EF8

Crystal structure of dihydroorotate dehydrogenase from Leishmania major in complex with Phenyl isothiocyanate

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 Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 401
ChainResidue
AALA19
AILE194
AASN195
AGLY223
AVAL226
ACYS249
AGLY250
AGLY251
AGLY272
ATHR273
AHOH504
AALA20
AHOH507
AHOH515
AHOH527
AGLY21
ALYS44
ASER45
AASN68
AMET70
AASN128
ALYS165

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 0FI A 402
ChainResidue
AGLY101
ALEU102
ASER103
AMET104
AASN107
APRO132
AVAL140
ACYS150

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AHIS160
ASER161

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
ATYR142
APHE144
AHOH584
AHOH807
AHOH808
BHIS174
BGOL404

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AILE203
AHOH593
BLEU227
BHOH593

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 0FI B 401
ChainResidue
BGLY101
BLEU102
BSER103
BMET104
BASN107
BPRO132
BVAL140
BCYS150

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 402
ChainResidue
BALA19
BALA20
BGLY21
BLYS44
BSER45
BASN68
BMET70
BASN128
BLYS165
BILE194
BASN195
BGLY222
BGLY223
BVAL226
BCYS249
BGLY250
BGLY251
BGLY272
BTHR273
BHOH502
BHOH509
BHOH514
BHOH516

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BSER103
BMET104
BARG105

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
AHIS174
AGOL404
AHOH742
BTYR142
BPHE144
BHOH592
BHOH786

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 405
ChainResidue
AHOH608
BILE203
BHOH573

223166

PDB entries from 2024-07-31

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