3H72

Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA

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)
A	SCOP2B Superfamily	Sialidases	8052060	3001607	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Sialidases	8052060	3001607	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	BNR_2	e3h72A1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: BNR_2	ECOD (1.6)
B	BNR_2	e3h72B1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: BNR_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.120.10.10	Mainly Beta	6 Propeller	Neuraminidase		CATH (4.3.0)
A	2.40.220.10	Mainly Beta	Beta Barrel	Intramolecular trans-sialidase	domain 3	CATH (4.3.0)
B	2.120.10.10	Mainly Beta	6 Propeller	Neuraminidase		CATH (4.3.0)
B	2.40.220.10	Mainly Beta	Beta Barrel	Intramolecular trans-sialidase	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02012	BNR/Asp-box repeat (BNR)	BNR/Asp-box repeat	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Sialidase A	hydrolase activity, acting on glycosyl bonds alpha-sialidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity exo-alpha-sialidase activity catalytic activity	carbohydrate metabolic process catabolic process oligosaccharide catabolic process oligosaccharide metabolic process carbohydrate catabolic process primary metabolic process metabolic process cellular process membrane lipid metabolic process sphingolipid catabolic process ceramide metabolic process ganglioside catabolic process carbohydrate derivative catabolic process glycosphingolipid catabolic process carbohydrate metabolic process catabolic process oligosaccharide catabolic process oligosaccharide metabolic process carbohydrate catabolic process primary metabolic process metabolic process cellular process membrane lipid metabolic process sphingolipid catabolic process ceramide metabolic process ganglioside catabolic process carbohydrate derivative catabolic process glycosphingolipid catabolic process lipid catabolic process glycolipid metabolic process glycosphingolipid metabolic process liposaccharide metabolic process carbohydrate derivative metabolic process sphingolipid metabolic process membrane lipid catabolic process glycolipid catabolic process ceramide catabolic process amide metabolic process ganglioside metabolic process lipid metabolic process	cellular anatomical structure membrane extracellular region membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle intracellular membrane-bounded organelle cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001791	Laminin G domain	Domain
A, B	IPR011040	Sialidase	Domain
A, B	IPR049964	Sialidase A repeat	Repeat
A, B	IPR023364	Trans-sialidase, domain 3	Homologous Superfamily
A, B	IPR036278	Sialidase superfamily	Homologous Superfamily
A, B	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A, B	IPR004124	Glycoside hydrolase, family 33, N-terminal	Domain
A, B	IPR005877	YSIRK Gram-positive signal peptide	Domain
A, B	IPR026856	Sialidase family	Family
A, B	IPR019931	LPXTG cell wall anchor 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.