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9DAQ

Structure of E. coli dihydrofolate reductase (DHFR) in an occluded conformation and in complex with a cycloguanil derivative

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004146molecular_functiondihydrofolate reductase activity
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005829cellular_componentcytosol
A0009257biological_process10-formyltetrahydrofolate biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0046452biological_processdihydrofolate metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046655biological_processfolic acid metabolic process
A0046656biological_processfolic acid biosynthetic process
A0050661molecular_functionNADP binding
A0051870molecular_functionmethotrexate binding
A0051871molecular_functiondihydrofolic acid binding
A0070401molecular_functionNADP+ binding
A0070402molecular_functionNADPH binding
Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT
ChainResidueDetails
AVAL13-THR35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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