Structure of PDB 4hzy Chain A

Receptor sequence
>4hzyA (length=388) Species: 489926 (Influenza A virus (A/swine/Missouri/2124514/2006(H2N3))) [Search protein sequence]
FRPFKSPLPLCPFRGFFPFHKDNAIRLGENKDVIVTREPYVSCDNDNCWS
FALAQGALLGTKHSNGTIKDRTPYRSLIRFPIGTAPVLGNYKEICIAWSS
SSCFDGKEWMHVCMTGNDNDASAQIIYGGRMTDSIKSWRKDILRTQESEC
QCIDGTCVVAVTDGPAANSADYRVYWIREGKIIKYENVPKTKIQYLEECS
CYVDIDVYCICRDNWKGSNRPWMRINNETILETGYVCSKFHSDTPRPADP
STMSCDSPSNVNGGPGVKGFGFKAGDDVWLGRTVSTSGRSGFEIIKVTEG
WINSPNHVKSITQTLVSNNDWSGYSGSFIVKAKDCFQPCFYVELIRGRPN
KNDDVSWTSNSIVTFCGLDNEPGSGNWPDGSNIGFMPK
3D structure
PDB4hzy Functional and structural analysis of influenza virus neuraminidase N3 offers further insight into the mechanisms of oseltamivir resistance.
ChainA
Resolution1.598 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D151 E277 R292 R371 Y406
Catalytic site (residue number reindexed from 1) D70 E198 R212 R289 Y324
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 D293 G297 D324 G345 D213 G217 D243 G263
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:4hzy, PDBe:4hzy, PDBj:4hzy
PDBsum4hzy
PubMed23824808
UniProtA9YN63

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