2AEQ

An epidemiologically significant epitope of a 1998 influenza virus neuraminidase forms a highly hydrated interface in the NA-antibody complex.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
IMGT Antibody Annotation
SAbDab Antibody Annotation
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	d2aeqa_	All beta proteins	6-bladed beta-propeller	Sialidases	Sialidases (neuraminidases)	automated matches	(Influenza A virus ) [TaxId: 11320 ],	SCOPe (2.08)
B [auth L]	d2aeql_	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	automated matches	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C [auth H]	d2aeqh_	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	V set domains (antibody variable domain-like)	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Sialidases (neuraminidases)	8071681	4002683	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Sialidases	8071682	3001607	SCOP2 (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	e2aeqA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: Neur	ECOD (1.6)
B [auth L]	V-set	e2aeqL1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set	ECOD (1.6)
C [auth H]	V-set_12	e2aeqH1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_12	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)
B [auth L]	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
C [auth H]	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)

IMGT Antibody Annotation IMGT Database Homepage

Chain	Protein Name	Description	Organism Name	Gene Allele Name(s)	Domain Name(s)	Receptor Type	Receptor Description	Provenance Source
B [auth L]	Mem5	L-KAPPA	Mus musculus (house mouse)	IGKV6-1501, IGKJ501, IGKC01, IGKC02	V-DOMAIN V-KAPPA, C-DOMAIN C-KAPPA	IG	FAB-GAMMA-2A_KAPPA	IMGT (202448-0)
C [auth H]	Mem5	VH-CH1	Mus musculus (house mouse)	IGHV7-302, IGHJ201, IGHG2A01, IGHG2A02	V-DOMAIN VH, C-DOMAIN CH1	IG	FAB-GAMMA-2A_KAPPA	IMGT (202448-0)

SAbDab Antibody Annotation SAbDab Database Homepage

Chain	Chain Class	Chain Subclass	Chain Type	Antigen Name(s)	Provenance Source
B [auth L]	Light Chain	IGKV6	Kappa	neuraminidase	SAbDab (2024-12-06)
C [auth H]	Heavy Chain	IGHV7	-	neuraminidase	SAbDab (2024-12-06)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00064	Neuraminidase (Neur)	Neuraminidase	-	Repeat
C [auth H]	PF07686	Immunoglobulin V-set domain (V-set)	Immunoglobulin V-set domain	This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	neuraminidase	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
B [auth L]	FAB light chain	-	-	-
C [auth H]	FAB heavy chain	binding antigen binding	adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains lymphocyte mediated immunity response to stimulus immune response immune system process B cell mediated immunity leukocyte mediated immunity immunoglobulin mediated immune response adaptive immune response immune effector process	protein-containing complex immunoglobulin complex cellular anatomical structure extracellular region

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
C [auth H]	IPR003597	Immunoglobulin C1-set	Domain
C [auth H]	IPR050199	Immunoglobulin Heavy Variable	Family
C [auth H]	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
C [auth H]	IPR036179	Immunoglobulin-like domain superfamily	Homologous Superfamily
C [auth H]	IPR013106	Immunoglobulin V-set domain	Domain
C [auth H]	IPR003599	Immunoglobulin domain subtype	Domain
C [auth H]	IPR007110	Immunoglobulin-like 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.