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1NSB

THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0033644cellular_componenthost cell membrane
A0046761biological_processviral budding from plasma membrane
A0055036cellular_componentvirion membrane
B0004308molecular_functionexo-alpha-sialidase activity
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0033644cellular_componenthost cell membrane
B0046761biological_processviral budding from plasma membrane
B0055036cellular_componentvirion membrane
Functional Information from PDB Data
site_idCHA
Number of Residues5
DetailsHIGH-AFFINITY CALCIUM-BINDING SITES
ChainResidue
AASP292
ATHR296
AASP323
AGLY343
AGLY345

site_idCHB
Number of Residues5
DetailsHIGH-AFFINITY CALCIUM-BINDING SITES
ChainResidue
BASP292
BTHR296
BASP323
BGLY343
BGLY345

site_idCLA
Number of Residues1
DetailsLOW-AFFINITY CALCIUM-BINDING SITES
ChainResidue
AGLU167

site_idCLB
Number of Residues1
DetailsLOW-AFFINITY CALCIUM-BINDING SITES
ChainResidue
BGLU167

site_idSIA
Number of Residues9
DetailsACTIVE SITE IN CHAINS A
ChainResidue
ATRP176
AILE220
AARG222
AGLU274
AARG291
AASP323
AARG115
AASP148
AARG149

site_idSIB
Number of Residues9
DetailsACTIVE SITE IN CHAINS B
ChainResidue
BARG115
BASP148
BARG149
BTRP176
BILE220
BARG222
BGLU274
BARG291
BASP323

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues754
DetailsRegion: {"description":"Head of neuraminidase","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1740114","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1740114","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1740114","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AASP148
AGLU275

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
BASP148
BGLU275

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PDB entries from 2025-12-17

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