Structure of PDB 4gzq Chain A

Receptor sequence
>4gzqA (length=388) Species: 119210 (H3N2 subtype) [Search protein sequence]
AEYRNWSKPQCDITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPDKCYQ
FALGQGTTLNNVHSNNTVRDRTPYRTLLMNELGVPFHLGTKQVCIAWSSS
SCHDGKAWLHVCITGDDKNATASFIYNGRLVDSVVSWSKEILRTQESECV
CINGTCTVVMTDGSASGKADTKILFIEEGKIVHTSTLSGSAQHVEECSCY
PRYPGVRCVCRDNWKGSNRPIVDINIKDHSIVSSYVCSGLVGDTPRKNDS
SSSSHCLDPNNEEGGHGVKGWAFDDGNDVWMGRTINETSRLGYETFKVIE
GWSNPKSKLQINRQVIVDRGNRSGYSGIFSVEGKSCINRCFYVELIRGRK
EETEVLWTSNSIVVFCGTSGTYGTGSWPDGADLNLMPI
3D structure
PDB4gzq Influenza virus neuraminidases with reduced enzymatic activity that avidly bind sialic Acid receptors.
ChainA
Resolution2.2 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 E196 R211 R290 Y325
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 SIA A R118 E119 D151 A246 E276 R292 R371 Y406 R37 E38 D70 A165 E195 R211 R290 Y325
BS02 CA A D293 G297 D324 G345 H347 D212 G216 D243 G264 H266
Gene Ontology
Molecular Function
GO:0004308 exo-alpha-sialidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0046761 viral budding from plasma membrane
Cellular Component
GO:0016020 membrane
GO:0020002 host cell plasma membrane
GO:0033644 host cell membrane
GO:0044423 virion component
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:4gzq, PDBe:4gzq, PDBj:4gzq
PDBsum4gzq
PubMed23015718
UniProtK7N5N3

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