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1NMC

COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 15 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE

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
N0004308molecular_functionexo-alpha-sialidase activity
N0005975biological_processcarbohydrate metabolic process
N0016020cellular_componentmembrane
N0033644cellular_componenthost cell membrane
N0046761biological_processviral budding from plasma membrane
N0055036cellular_componentvirion membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues756
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 Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23429702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7549872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8371267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9342319","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23429702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7549872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9342319","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 828
ChainResidueDetails
AASP151activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor
AGLU277activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AARG292electrostatic stabiliser
AARG371electrostatic stabiliser
ATYR406electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 828
ChainResidueDetails

site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
NASP151
NGLU277

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AASP151
AGLU277

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
NGLU277
NASP151
NARG220
NTRP412
NARG371

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AGLU277
AASP151
AARG220
ATRP412
AARG371

245011

PDB entries from 2025-11-19

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