2OIP

Crystal Structure of the S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2oipa1	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
A	d2oipa2	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
C	d2oipc1	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
C	d2oipc2	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
D	d2oipd1	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
D	d2oipd2	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
E	d2oipe1	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
E	d2oipe2	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
B	d2oipb1	Alpha and beta proteins (a/b)	Dihydrofolate reductase-like	Dihydrofolate reductase-like	automated matches	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)
B	d2oipb2	Alpha and beta proteins (a+b)	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	Thymidylate synthase/dCMP hydroxymethylase	automated matches	(Cryptosporidium hominis ) [TaxId: 237895 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Thymidylat_synt	e2oipA2	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: Thymidylat_synt	ECOD (1.6)
A	DHFR_1	e2oipA3	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	Thymidylat_synt	e2oipC1	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: Thymidylat_synt	ECOD (1.6)
C	DHFR_1	e2oipC2	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	Thymidylat_synt	e2oipD2	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: Thymidylat_synt	ECOD (1.6)
D	DHFR_1	e2oipD3	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	Thymidylat_synt	e2oipE2	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: Thymidylat_synt	ECOD (1.6)
E	DHFR_1	e2oipE3	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	Thymidylat_synt	e2oipB2	A: a+b two layers	X: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	H: Thymidylate synthase/dCMP hydroxymethylase (From Topology)	T: Thymidylate synthase/dCMP hydroxymethylase	F: Thymidylat_synt	ECOD (1.6)
B	DHFR_1	e2oipB3	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)
A	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain 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)
C	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain 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)
D	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain 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)
E	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain 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)
B	3.30.572.10	Alpha Beta	2-Layer Sandwich	Thymidylate Synthase	Chain A	CATH (4.3.0)

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.