Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1W21

Structure of Neuraminidase from English duck subtype N6 complexed with 30 mM sialic acid (NANA, Neu5Ac), crystal soaked for 43 hours at 291 K.

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
BASP1157
BGLU1284

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
CGLU2284
CASP2157

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
DASP3157
DGLU3284

249524

PDB entries from 2026-02-18

PDB statisticsPDBj update infoContact PDBjnumon