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7F3Y

Wild-type Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) complexed with methotrexate (MTX), NADPH and dUMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004146molecular_functiondihydrofolate reductase activity
A0004799molecular_functionthymidylate synthase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006231biological_processdTMP biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0009165biological_processnucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016741molecular_functiontransferase activity, transferring one-carbon groups
A0032259biological_processmethylation
A0046654biological_processtetrahydrofolate biosynthetic process
B0003824molecular_functioncatalytic activity
B0004146molecular_functiondihydrofolate reductase activity
B0004799molecular_functionthymidylate synthase activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006231biological_processdTMP biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0009165biological_processnucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016741molecular_functiontransferase activity, transferring one-carbon groups
B0032259biological_processmethylation
B0046654biological_processtetrahydrofolate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues24
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GLGnkgvLPWkcnslDmkyFcavT
ChainResidueDetails
AGLY39-THR62

site_idPS00091
Number of Residues29
DetailsTHYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriLlcaWNvkdldqma.....LpPCHilcQFyV
ChainResidueDetails
AARG470-VAL498

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS490
BCYS490

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING:
ChainResidueDetails
AILE14
AGLY165
ATYR170
AARG345
AHIS491
AGLN509
AASN521
AHIS551
BILE14
BALA16
BGLY39
AALA16
BASP54
BARG106
BSER108
BSER128
BASN144
BILE164
BGLY165
BTYR170
BARG345
BHIS491
AGLY39
BGLN509
BASN521
BHIS551
AASP54
AARG106
ASER108
ASER128
AASN144
AILE164

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL31
ATHR185
BVAL31
BTHR185

237423

PDB entries from 2025-06-11

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