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1AI9

CANDIDA ALBICANS DIHYDROFOLATE REDUCTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005739cellular_componentmitochondrion
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0050661molecular_functionNADP binding
B0004146molecular_functiondihydrofolate reductase activity
B0005739cellular_componentmitochondrion
B0006730biological_processone-carbon metabolic process
B0016491molecular_functionoxidoreductase activity
B0046452biological_processdihydrofolate metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046655biological_processfolic acid metabolic process
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP A 193
ChainResidue
AVAL10
AARG56
ALYS57
ATHR58
ALEU77
ASER78
AARG79
ASER94
AILE112
AGLY114
AALA115
AALA11
AGLU116
AILE117
ATYR118
AGLU120
AHOH360
AILE19
AGLY23
ALYS24
AMET25
AARG30
ALYS31
AGLY55

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NDP B 193
ChainResidue
BALA11
BILE19
BGLY20
BLYS22
BGLY23
BLYS24
BMET25
BGLY55
BARG56
BLYS57
BTHR58
BLEU77
BSER78
BARG79
BSER94
BSER95
BILE112
BGLY114
BALA115
BGLU116
BILE117
BTYR118
BGLU120
BHOH231
BHOH322
BHOH323
BHOH343
BHOH350

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGykgkMPWrlrk.EiryFkdvT
ChainResidueDetails
AGLY18-THR40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues372
DetailsDomain: {"description":"DHFR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00660","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11520201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11520201","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0ABQ4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1ra2
ChainResidueDetails
AVAL10
AGLU32
AILE33
AMET25
AILE112
ALEU69
APHE36

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1ra2
ChainResidueDetails
BVAL10
BGLU32
BILE33
BMET25
BILE112
BLEU69
BPHE36

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PDB entries from 2025-12-24

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