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1V0Z

Structure of Neuraminidase from English duck subtype N6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0033644cellular_componenthost cell membrane
A0055036cellular_componentvirion membrane
B0004308molecular_functionexo-alpha-sialidase activity
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0033644cellular_componenthost cell membrane
B0055036cellular_componentvirion membrane
C0004308molecular_functionexo-alpha-sialidase activity
C0005975biological_processcarbohydrate metabolic process
C0016020cellular_componentmembrane
C0033644cellular_componenthost cell membrane
C0055036cellular_componentvirion membrane
D0004308molecular_functionexo-alpha-sialidase activity
D0005975biological_processcarbohydrate metabolic process
D0016020cellular_componentmembrane
D0033644cellular_componenthost cell membrane
D0055036cellular_componentvirion membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1516
DetailsRegion: {"description":"Head of neuraminidase","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2004","submissionDatabase":"PDB data bank","title":"The crystal structure of influenza type A virus neuraminidase of the N6 subtype at 1.85 A resolution.","authors":["Rudino-Pinera E.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"The crystal structure of type A influenza virus neuraminidase of the N6 subtype reveals the existence of two separate Neu5Ac binding sites.","authors":["Rudino-Pinera E.","Tunnah P.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2004","submissionDatabase":"PDB data bank","title":"The crystal structure of influenza type A virus neuraminidase of the N6 subtype at 1.85 A resolution.","authors":["Rudino-Pinera E.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"The crystal structure of type A influenza virus neuraminidase of the N6 subtype reveals the existence of two separate Neu5Ac binding sites.","authors":["Rudino-Pinera E.","Tunnah P.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2004","submissionDatabase":"PDB data bank","title":"The crystal structure of influenza type A virus neuraminidase of the N6 subtype at 1.85 A resolution.","authors":["Rudino-Pinera E.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2004","submissionDatabase":"PDB data bank","title":"The crystal structure of influenza type A virus neuraminidase of the N6 subtype at 1.85 A resolution.","authors":["Rudino-Pinera E.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"PDB data bank","title":"The crystal structure of type A influenza virus neuraminidase of the N6 subtype reveals the existence of two separate Neu5Ac binding sites.","authors":["Rudino-Pinera E.","Tunnah P.","Crennell S.J.","Webster R.G.","Laver W.G.","Garman E.F."]}}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AASP157
AGLU284

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
BASP157
BGLU284

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
CASP157
CGLU284

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
DASP157
DGLU284

239492

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