Structure of PDB 3k39 Chain D

Receptor sequence
>3k39D (length=389) Species: 343983 (Influenza B virus (B/Perth/211/2001)) [Search protein sequence]
PEWTYPRLSCPGSTFQKALLISPHRFGETKGNSAPLIIREPFIACGPKEC
KHFALTHYAAQPGGYYNGTRGDRNKLRHLISVKLGKIPTVENSIFHMAAW
SGSACHDGKEWTYIGVDGPENNALLKIKYGEAYTDTYHSYANNILRTQES
ACNCIGGNCYLMITDGSASGISECRFLKIREGRIIKEIFPTGRVKHTEEC
TCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTETYLDTPR
PDDGSITGPCESNGDKGSGGIKGGFVHQRMASKIGRWYSRTMSKTKRMGM
GLYVKYDGDPWTDSDALALSGVMVSMEEPGWYSFGFEIKDKKCDVPCIGI
EMVHDGGKETWHSAATAIYCLMGSGQLLWDTVTGVDMAL
3D structure
PDB3k39 Structural and Functional Basis of Resistance to Neuraminidase Inhibitors of Influenza B Viruses.
ChainD
Resolution2.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D149 E276 R292 R374 Y409
Catalytic site (residue number reindexed from 1) D72 E199 R215 R297 Y332
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 D D293 T297 D324 G344 G346 D216 T220 D247 G267 G269
BS02 BCZ D R116 E117 D149 R223 E226 E275 R292 R374 Y409 R39 E40 D72 R146 E149 E198 R215 R297 Y332
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:3k39, PDBe:3k39, PDBj:3k39
PDBsum3k39
PubMed20695427
UniProtQ3S340

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