2W9S

Staphylococcus aureus S1:DHFR in complex with trimethoprim

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
AMR Gene: CARD Annotation
AMR Gene Family: CARD Annotation
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	d2w9sa_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d2w9sb_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
C	d2w9sc_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
E	d2w9se_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
F	d2w9sf_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
D	d2w9sd_	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Staphylococcus aureus ) [TaxId: 1280 ],	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	8068958	4000755	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Dihydrofolate reductase-like	8068959	3001255	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Dihydrofolate reductase-like	8068959	3001255	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Dihydrofolate reductase-like	8068959	3001255	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Dihydrofolate reductase-like	8068959	3001255	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Dihydrofolate reductase-like	8068959	3001255	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Dihydrofolate reductase-like	8068959	3001255	SCOP2B (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	e2w9sA1	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)
B	DHFR_1	e2w9sB1	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)
C	DHFR_1	e2w9sC1	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)
E	DHFR_1	e2w9sE1	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)
F	DHFR_1	e2w9sF1	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)
D	DHFR_1	e2w9sD1	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
B	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
C	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
E	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
F	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)
D	3.40.430.10	Alpha Beta	3-Layer(aba) Sandwich	Dihydrofolate Reductase, subunit A	Dihydrofolate Reductase, subunit A	CATH (4.3.0)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A, B, C, D, E A, B, C, D, E, F	ARO:3002865	dfrC	dfrC is a chromosome-encoded dihydrofolate reductase found in Staphylococcus aureus.	CARD (3.3.0)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A, B, C, D, E A, B, C, D, E, F	ARO:3001218	trimethoprim resistant dihydrofolate reductase dfr	diaminopyrimidine antibiotic	antibiotic target replacement	CARD (3.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	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, B, C, D, E A, B, C, D, E, F	DIHYDROFOLATE REDUCTASE TYPE 1 FROM TN4003	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule 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 methotrexate response to stimulus response to chemical response to oxygen-containing compound response to nitrogen compound response to organic cyclic 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 methotrexate response to stimulus response to chemical response to oxygen-containing compound response to nitrogen compound response to organic cyclic 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 folic acid-containing compound biosynthetic process modified amino acid biosynthetic process biosynthetic process pteridine-containing compound biosynthetic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR017925	Dihydrofolate reductase conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR012259	Dihydrofolate reductase	Family
A, B, C, D, E A, B, C, D, E, F	IPR024072	Dihydrofolate reductase-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	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.