9DAR | pdb_00009dar

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

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Dihydrofolate reductase-like	8032695	3001255	SCOP2B (2022-06-29)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00186	Dihydrofolate reductase (DHFR_1)	Dihydrofolate reductase		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Dihydrofolate reductase	amide binding organic acid binding binding ion binding anion binding carboxylic acid binding heterocyclic compound binding methotrexate binding small molecule binding NADP+ binding nucleotide binding nucleoside phosphate binding purine nucleotide binding adenyl nucleotide binding amide binding organic acid binding binding ion binding anion binding carboxylic acid binding heterocyclic compound binding methotrexate binding small molecule binding NADP+ binding nucleotide binding nucleoside phosphate binding purine nucleotide binding adenyl nucleotide binding NADP binding dihydrofolic acid binding modified amino acid binding NADPH binding vitamin binding folic acid binding dihydrofolate reductase activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors catalytic activity	response to stimulus response to chemical response to xenobiotic stimulus response to methotrexate response to oxygen-containing compound response to nitrogen compound small molecule metabolic process metabolic process cellular process one-carbon metabolic process oxoacid metabolic process dicarboxylic acid metabolic process dihydrofolate metabolic process carboxylic acid metabolic process response to stimulus response to chemical response to xenobiotic stimulus response to methotrexate response to oxygen-containing compound response to nitrogen compound small molecule metabolic process metabolic process cellular process one-carbon metabolic process oxoacid metabolic process dicarboxylic acid metabolic process dihydrofolate metabolic process carboxylic acid metabolic process modified amino acid metabolic process organic acid metabolic process folic acid-containing compound metabolic process pteridine-containing compound metabolic process vitamin metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process response to antibiotic modified amino acid biosynthetic process vitamin biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process dicarboxylic acid biosynthetic process folic acid biosynthetic process folic acid-containing compound biosynthetic process water-soluble vitamin biosynthetic process small molecule biosynthetic process amide biosynthetic process biosynthetic process pteridine-containing compound biosynthetic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process 10-formyltetrahydrofolate metabolic process 10-formyltetrahydrofolate biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017925	Dihydrofolate reductase conserved site	Conserved Site
A	IPR012259	Dihydrofolate reductase	Family
A	IPR024072	Dihydrofolate reductase-like domain superfamily	Homologous Superfamily
A	IPR001796	Dihydrofolate reductase domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.