Structure of PDB 3tia Chain D

Receptor sequence
>3tiaD (length=388) Species: 382827 (Influenza A virus (A/RI/5+/1957(H2N2))) [Search protein sequence]
VEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPGKCYQ
FALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSSS
SCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECV
CINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLSGSAQHIEECSCY
PRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDS
SSNSNCRNPNNERGTQGVKGWAFDNGNDLWMGRTISKESRSGYETFKVIG
GWSTPNSKSQVNRQVIVDNNNWSGYSGIFSVEGKSCINRCFYVELIRGRP
QETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
3D structure
PDB3tia Structural and functional analysis of laninamivir and its octanoate prodrug reveals group specific mechanisms for influenza NA inhibition
ChainD
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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 BMA D Q391 V392 R394 Q310 V311 R313
BS02 MAN D Q391 R394 Q310 R313
BS03 CA D D293 G297 D324 G345 Q347 D212 G216 D243 G264 Q266
BS04 LNV D R118 E119 D151 R152 W178 E276 R292 R371 Y406 R37 E38 D70 R71 W97 E195 R211 R290 Y325 MOAD: ic50=3.12nM
BindingDB: IC50=3100nM
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:3tia, PDBe:3tia, PDBj:3tia
PDBsum3tia
PubMed22028647
UniProtQ194T1

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