1PD9

Analysis of Three Crystal Structure Determinations of a 5-Methyl-6-N-Methylanilino Pyridopyrimidine antifolate Complex with Human Dihydrofolate Reductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
A	0003723	molecular_function	RNA binding
A	0003729	molecular_function	mRNA binding
A	0004146	molecular_function	dihydrofolate reductase activity
A	0005542	molecular_function	folic acid binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0008144	molecular_function	obsolete drug binding
A	0016491	molecular_function	oxidoreductase activity
A	0017148	biological_process	negative regulation of translation
A	0031103	biological_process	axon regeneration
A	0031427	biological_process	response to methotrexate
A	0046452	biological_process	dihydrofolate metabolic process
A	0046653	biological_process	tetrahydrofolate metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046655	biological_process	folic acid metabolic process
A	0050661	molecular_function	NADP binding
A	0051000	biological_process	positive regulation of nitric-oxide synthase activity
A	0070402	molecular_function	NADPH binding
A	1990825	molecular_function	sequence-specific mRNA binding
A	2000121	biological_process	regulation of removal of superoxide radicals

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

site_id	PS00075
Number of Residues	24
Details	DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfryFqrmT

Chain	Residue	Details
A	GLY15-THR38

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:15039552, ECO:0000269\|PubMed:16222560, ECO:0000269\|PubMed:19478082

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf