Structure of PDB 4cpz Chain H

Receptor sequence
>4cpzH (length=390) Species: 11520 (Influenza B virus) [Search protein sequence]
EPEWTYPRLSCPGSTFQKALLISPHRFGETKGNSAPLIIREPFIACGPNE
CKHFALTHYAAQPGGYYNGTRGDRNKLRHLISVKLGKIPTVENSIFHMAA
WSGSACHDGKEWTYIGVDGPDNDALLKVKYGEAYTDTYHSYANKLLRTQE
SACNCIGGNCYLMITDGSASGVSECRFLKIREGRIIKEIFPTGRVKHTEE
CTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTDTYLDTP
RPDDGSITGPCESNGDKGSGGIKGGFVHQRMESKIGRWYSRTMSKTERMG
MGLYVKYDGDPWADSDALAFSGVMVSMKEPGWYSFGFEIKDKECDVPCIG
IEMVHDGGKETWHSAATAIYCLMGSGQLLWDTVTGVDMAL
3D structure
PDB4cpz A Novel I221 L Substitution in Neuraminidase Confers High Level Resistance to Oseltamivir in Influenza B Viruses.
ChainH
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) 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 H D292 T296 D323 G343 G345 D217 T221 D248 G268 G270
BS02 ZMR H R115 E116 D148 W176 E225 E274 R291 R373 Y408 R40 E41 D73 W101 E150 E199 R216 R298 Y333 MOAD: Ki=20.85nM
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:4cpz, PDBe:4cpz, PDBj:4cpz
PDBsum4cpz
PubMed24795482
UniProtU5XBU0

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