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9OOI

Crystal structure of dihydrofolate reductase (DHFR) from the filarial nematode W. bancrofti in complex with NADPH and antifolate 2-({4-[(2-amino-4-oxo-4,7-dihydro-1H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]benzene-1-carbonyl}amino)benzoic acid (OG7 or TSD001)

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
C0004146molecular_functiondihydrofolate reductase activity
C0005739cellular_componentmitochondrion
C0006730biological_processone-carbon metabolic process
C0016491molecular_functionoxidoreductase activity
C0046452biological_processdihydrofolate metabolic process
C0046654biological_processtetrahydrofolate biosynthetic process
C0046655biological_processfolic acid metabolic process
C0050661molecular_functionNADP binding
Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGrnggMPWflpa.EmarFaklT
ChainResidueDetails
AGLY18-THR40

245663

PDB entries from 2025-12-03

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