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8F09

Crystal structure of a trimethoprim-resistant dihydrofolate reductase (DHFR) enzyme from an uncultured soil bacterium

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0042398biological_processmodified amino acid biosynthetic process
A0042559biological_processpteridine-containing compound biosynthetic process
A0043168molecular_functionanion binding
A0044281biological_processsmall molecule metabolic process
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0050661molecular_functionNADP binding
B0004146molecular_functiondihydrofolate reductase activity
B0006730biological_processone-carbon metabolic process
B0016491molecular_functionoxidoreductase activity
B0042398biological_processmodified amino acid biosynthetic process
B0042559biological_processpteridine-containing compound biosynthetic process
B0043168molecular_functionanion binding
B0044281biological_processsmall molecule metabolic process
B0046452biological_processdihydrofolate metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046655biological_processfolic acid metabolic process
B0050661molecular_functionNADP binding
Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGksndLPWhlpd.DmkyFmqtT
ChainResidueDetails
AVAL14-THR36

237423

PDB entries from 2025-06-11

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