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8SZE

Crystal structure of Yersinia pestis dihydrofolate reductase in complex with Trimethoprim

Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016491molecular_functionoxidoreductase activity
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
B0004146molecular_functiondihydrofolate reductase activity
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016491molecular_functionoxidoreductase activity
B0046452biological_processdihydrofolate metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046655biological_processfolic acid metabolic process
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWhlpa.DlawFkrnT
ChainResidueDetails
AVAL14-THR36

224931

PDB entries from 2024-09-11

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