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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad7nn9a_ 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

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilySialidases 8032977 3001607 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ANeure7nn9A1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 6-bladedF: NeurECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.120.10.10 Mainly Beta 6 Propeller Neuraminidase CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00064Neuraminidase (Neur)Neuraminidase- Repeat

InterPro: Protein Family Classification InterPro Database Homepage

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

ChainsEnzyme NameDescriptionCatalytic Residues
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]
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