7NN9

NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN)

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d7nn9a_	All beta proteins	6-bladed beta-propeller	Sialidases	Sialidases (neuraminidases)	Influenza neuraminidase	(Influenza A virus (A/tern/Australia/G70C/1975(H11N9)) ) [TaxId: 384509 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Sialidases	8032977	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	Neur	e7nn9A1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: Neur	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00064	Neuraminidase (Neur)	Neuraminidase	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	NEURAMINIDASE N9	cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process primary metabolic process metabolic process cellular process biological process involved in interspecies interaction between organisms non-lytic viral release viral budding viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction virion assembly exit from host cell viral process viral budding from plasma membrane carbohydrate metabolic process primary metabolic process metabolic process cellular process biological process involved in interspecies interaction between organisms non-lytic viral release viral budding viral life cycle biological process involved in interaction with host biological process involved in symbiotic interaction virion assembly exit from host cell viral process viral budding from plasma membrane viral release from host cell	cellular anatomical structure membrane host cell plasma membrane host cellular component host cell part host cell membrane virion component virion membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001860	Glycoside hydrolase, family 34	Family
A	IPR033654	Sialidase, Influenza viruses A/B	Domain
A	IPR036278	Sialidase superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	exo-alpha-sialidase (GH34 Family) M-CSA #828	The influenza virus neuramidase is a concanovin A-like lectin/glucanase. This glycoside hydrolase is composed of a central, veta-propeller catalytic domain flanked by two lectin-like domains. NA is involved in the pathogenesis of cholera by removing sialic acid from higher order gangliosides to unmask GM1, the receptor for the cholera toxin. The enzyme catalyses the hydrolysis of glycoside linkages between terminal sialic acids and adjacent sugar moieties. NA presents an excellent target for drug design against cholera.	Defined by 5 residues: ASP:A-70 [auth A-151]GLU:A-197 [auth A-277]ARG:A-212 [auth A-292]ARG:A-290 [auth A-371]TYR:A-324 [auth A-406] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.2.1.18 (PDB Primary Data) Search M-CSA Motif + EC 3.2.1.18

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.