Structure of PDB 4cpn Chain A

Receptor sequence
>4cpnA (length=390) Species: 604436 (Influenza B virus (B/Brisbane/60/2008)) [Search protein sequence]
EPEWTYPRLSCPGSTFQKALLISPHRFGETKGNSAPLIIREPFIACGPNE
CKHFALTHYAAQPGGYYNGTRGDRNKLRHLISVKLGKIPTVENSIFHMAA
WSGSACHDGKEWTYIGVDGPDNNALLKVKYGEAYTDTYHSYANKILRTQE
SACNCIGGNCYLMITDGSASGVSECRFLKIREGRIIKEIFPTGRVKHTEE
CTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTDTYLDTP
RPNDGSITGPCESNGDKGSGGIKGGFVHQRMESKIGRWYSRTMSKTERMG
MGLYVKYDGDPWADSDALAFSGVMVSMKEPGWYSFGFEIKDKKCDVPCIG
IEMVHDGGKETWHSAATAIYCLMGSGQLLWDTVTGVDMAL
3D structure
PDB4cpn A Novel I221 L Substitution in Neuraminidase Confers High Level Resistance to Oseltamivir in Influenza B Viruses.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D148 E275 R291 R373 Y408
Catalytic site (residue number reindexed from 1) D73 E200 R216 R298 Y333
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 A D292 T296 D323 G343 G345 D217 T221 D248 G268 G270
BS02 ZMR A R115 E116 D148 R149 W176 R222 E225 A244 E274 E275 R291 R373 Y408 R40 E41 D73 R74 W101 R147 E150 A169 E199 E200 R216 R298 Y333
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
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:4cpn, PDBe:4cpn, PDBj:4cpn
PDBsum4cpn
PubMed24795482
UniProtC0LT34

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