Structure of PDB 1xog Chain A

Receptor sequence
>1xogA (length=387) Species: 11320 (Influenza A virus) [Search protein sequence]
DFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFY
ALSQGTTIRGKHSNGTIHDRSQYRALISWPLSSPPTVYNSRVECIGWSST
SCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECV
CHNGVCPVVFTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCY
GERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYICSPVLTDNPRPNDP
TVGKCNDPYPGNNNNGVKGFSYLDGVNTWLGRTISIASRSGYEMLKVPNA
LTDDKSKPTQGQTIVLNTDWSGYSGSFMDYWAEGECYRACFYVELIRGRP
KEDKVWWTSNSIVSMCSSTEFLGQWDWPDGAKIEYFL
3D structure
PDB1xog Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D152 E279 R294 R372 Y406
Catalytic site (residue number reindexed from 1) D69 E196 R211 R289 Y323
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 ABW A E120 D152 R153 W180 E278 R294 R372 Y406 E37 D69 R70 W97 E195 R211 R289 Y323 PDBbind-CN: -logKd/Ki=6.39,IC50=410nM
Gene Ontology
Molecular Function
GO:0004308 exo-alpha-sialidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0046761 viral budding from plasma membrane
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:1xog, PDBe:1xog, PDBj:1xog
PDBsum1xog
PubMed15582424
UniProtP03472|NRAM_I75A5 Neuraminidase (Gene Name=NA)

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