1SYR

Initial Structural Analysis of Plasmodium falciparum thioredoxin

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d1syra_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
B	d1syrb_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
C	d1syrc_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
D	d1syrd_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
E	d1syre_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
F	d1syrf_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
G	d1syrg_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
H	d1syrh_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
I	d1syri_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
J	d1syrj_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
K	d1syrk_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
L	d1syrl_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Thioltransferase	Thioredoxin	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Thioltransferase	8029245	4000237	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioredoxin-like	8041624	3000031	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Thioredoxin-like	8041624	3000031	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	Thioredoxin	e1syrA1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
B	Thioredoxin	e1syrB1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
C	Thioredoxin	e1syrC1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
D	Thioredoxin	e1syrD1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
E	Thioredoxin	e1syrE1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
F	Thioredoxin	e1syrF1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
G	Thioredoxin	e1syrG1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
H	Thioredoxin	e1syrH1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
I	Thioredoxin	e1syrI1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
J	Thioredoxin	e1syrJ1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
K	Thioredoxin	e1syrK1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)
L	Thioredoxin	e1syrL1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: Thioredoxin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
C	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
D	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
E	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
F	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
G	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
H	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
I	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
J	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
K	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
L	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	PF00085	Thioredoxin (Thioredoxin)	Thioredoxin	Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.	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, G, H, I, J, K, L	thioredoxin	oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity oxidoreductase activity catalytic activity, acting on a protein protein-disulfide reductase activity catalytic activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR017937	Thioredoxin, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR013766	Thioredoxin domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR005746	Thioredoxin	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.