6XG5

X-ray structure of Escherichia coli dihydrofolate reductase in complex with trimethoprim

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004146	molecular_function	dihydrofolate reductase activity
A	0005515	molecular_function	protein binding
A	0005542	molecular_function	folic acid binding
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0009257	biological_process	10-formyltetrahydrofolate biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016491	molecular_function	oxidoreductase activity
A	0031427	biological_process	response to methotrexate
A	0046452	biological_process	dihydrofolate metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046655	biological_process	folic acid metabolic process
A	0046656	biological_process	folic acid biosynthetic process
A	0046677	biological_process	response to antibiotic
A	0050661	molecular_function	NADP binding
A	0051870	molecular_function	methotrexate binding
A	0051871	molecular_function	dihydrofolic acid binding
A	0070401	molecular_function	NADP+ binding
A	0070402	molecular_function	NADPH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue NDP A 301

site_id	AC2
Number of Residues	7
Details	binding site for residue GOL A 302

site_id	AC3
Number of Residues	13
Details	binding site for residue TOP A 303

Chain	Residue
A	ARG98

Functional Information from PROSITE/UniProt

site_id	PS00075
Number of Residues	23
Details	DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT

Chain	Residue	Details
A	VAL13-THR35

Functional Information from SwissProt/UniProt