Structure of PDB 4k1j Chain B

Receptor sequence
>4k1jB (length=388) Species: 382827 (Influenza A virus (A/RI/5+/1957(H2N2))) [Search protein sequence]
VEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPGKCYQ
FALGQGTTLDNKHSNGTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSSS
SCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECV
CINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLSGSAQHIEECSCY
PRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDS
SSNSNCRNPNNERGTQGVKGWAFDNGNDLWMGRTISKESRSGYETFKVIG
GWSTPNSKSQVNRQVIVDNNNWSGYSGIFSVEGKSCINRCFYVELIRGRP
QETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
3D structure
PDB4k1j Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding
ChainB
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 CA B D293 G297 D324 G345 Q347 D212 G216 D243 G264 Q266
BS02 G39 B R118 E119 D151 W178 R224 E276 R292 N294 R371 Y406 R37 E38 D70 W97 R143 E195 R211 N213 R290 Y325
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:4k1j, PDBe:4k1j, PDBj:4k1j
PDBsum4k1j
PubMed23531861
UniProtQ194T1

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