Structure of PDB 4fvk Chain A

Receptor sequence
>4fvkA (length=367) Species: 1129345 (Influenza A virus (A/little yellow-shouldered bat/Guatemala/153/2009(H17N10))) [Search protein sequence]
FYWRAKSQMCEVKGWVPTHRGFPWGPELPGDLILSRRAYVSCDLTSCFKF
FIAYGLSANQHLLNTSMEWEESLYKTPIGSASTLSTSEMILPGRSSSACF
DGLKWTVLVANGRDRNSFIMIKYGEEVTDTFSASRGGPLRLPNSECICIE
GSCFVIVSDGPNVNQSVHRIYELQNGTVQRWKQLNTTGINFEYSTCYTIN
NLIKCTGTNLWNDAKRPLLRFTKELNYQIVEPCNGAPTDFPRGGLTTPSC
KMAQEKGEGGIQGFILDEKPAWTSKTKAESSQNGFVLEQIPNGIESEGTV
SLSYELFSNKRTGRSGFFQPKGDLISGCQRICFWLEIEDQTVGLGMIQEL
STFCGINSPVQNINWDS
3D structure
PDB4fvk Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus
ChainA
Resolution2.198 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W154 Y277 T292 Q371 R406
Catalytic site (residue number reindexed from 1) W69 Y193 T208 Q282 R314
Enzyme Commision number 3.2.1.18: exo-alpha-sialidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A N293 D297 D324 G345 G347 N209 D213 D239 G257 G259
BS02 ZN A E386 T388 E297 T299
BS03 ZN A W154 E156 W69 E71
Gene Ontology
Molecular Function
GO:0004308 exo-alpha-sialidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane
GO:0033644 host cell membrane
GO:0055036 virion membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4fvk, PDBe:4fvk, PDBj:4fvk
PDBsum4fvk
PubMed23012237
UniProtH6QM75

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