Structure of PDB 3o9j Chain A

Receptor sequence
>3o9jA (length=387) Species: 385580 (Influenza A virus (A/duck/Ukraine/1/1963(H3N8))) [Search protein sequence]
TYMNNTEAICDAKGFAPFSKDNGIRIGSRGHIFVIREPFVSCSPIECRTF
FLTQGSLLNDKHSNGTVKDRSPFRTLMSVEVGQSPNVYQARFEAVAWSAT
ACHDGKKWMTVGVTGPDSKAVAVIHYGGVPTDVVNSWAGDILRTQESSCT
CIQGDCYWVMTDGPANRQAQYRIYKANQGRIIGQTDISFNGGHIEECSCY
PNDGKVECVCRDNWTGTNRPVLVISPDLSYRVGYLCAGIPSDTPRGEDTQ
FTGSCTSPMGNQGYGVKGFGFRQGTDVWMGRTISRTSRSGFEILRIKNGW
TQTSKEQIRKQVVVDNLNWSGYSGSFTLPVELSGKDCLVPCFWVEMIRGK
PEEKTIWTSSSSIVMCGVDYEVADWSWHDGAILPFDI
3D structure
PDB3o9j Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.
ChainA
Resolution2.0002 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 E279 R294 R376 Y411
Catalytic site (residue number reindexed from 1) D69 E196 R211 R288 Y322
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 RP6 A R118 R152 W180 A248 E278 R294 R376 Y411 R36 R70 W97 A165 E195 R211 R288 Y322
BS02 CA A D295 G299 D326 Y352 D212 G216 D242 Y264
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:3o9j, PDBe:3o9j, PDBj:3o9j
PDBsum3o9j
PubMed21081911
UniProtQ07599|NRAM_I63A3 Neuraminidase (Gene Name=NA)

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