3ETN

Crystal structure of putative phosphosugar isomerase involved in capsule formation (YP_209877.1) from Bacteroides fragilis NCTC 9343 at 1.70 A resolution

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8085887	3001397	SCOP2B (2022-06-29)
A	SCOP2 Family	mono-SIS domain	8085886	4003354	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SIS domain/Ribosomal protein S2-like	8085887	3001397	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8085887	3001397	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SIS domain/Ribosomal protein S2-like	8085887	3001397	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)
C	SIS	e3etnC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)
A	SIS	e3etnA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)
B	SIS	e3etnB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)
D	SIS	e3etnD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: SIS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
A	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
B	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
D	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01380	SIS domain (SIS)	SIS domain	SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domain ...	SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	putative phosphosugar isomerase involved in capsule formation	isomerase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses intramolecular oxidoreductase activity arabinose-5-phosphate isomerase activity catalytic activity binding carbohydrate derivative binding	carbohydrate derivative metabolic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR046348	SIS domain superfamily	Homologous Superfamily
A, B, C, D	IPR001347	SIS domain	Domain
A, B, C, D	IPR035474	KpsF-like, SIS 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.