6UWQ

Crystal structure of dihydrofolate reductase from Mycobacterium ulcerans with SDDC-0001565 inhibitor

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6uwqa_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	Dihydrofolate reductases	automated matches	(Mycobacterium ulcerans Agy99 ) [TaxId: 362242 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Dihydrofolate reductases	8101342	4000755	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Dihydrofolate reductase-like	8101343	3001255	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DHFR_1	e6uwqA1	A: a/b three-layered sandwiches	X: Dihydrofolate reductases (From Topology)	H: Dihydrofolate reductases (From Topology)	T: Dihydrofolate reductases	F: DHFR_1	ECOD (1.6)

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	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 binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding	small molecule metabolic process metabolic process cellular process one-carbon metabolic process folic acid-containing compound biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process tetrahydrofolate biosynthetic process pteridine-containing compound metabolic process tetrahydrofolate metabolic process oxoacid metabolic process small molecule metabolic process metabolic process cellular process one-carbon metabolic process folic acid-containing compound biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process tetrahydrofolate biosynthetic process pteridine-containing compound metabolic process tetrahydrofolate metabolic process oxoacid metabolic process dicarboxylic acid metabolic process dihydrofolate metabolic process carboxylic acid metabolic process organic acid metabolic process vitamin metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

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

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.