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1MWE

THE X-RAY STRUCTURE OF A COMPLEX OF TERN N9 INFLUENZA VIRUS NEURAMINIDASE COMPLEXED WITH SIALIC ACID AT 4 DEGREES C REVEALING A SECOND SIALIC ACID BINDING SITE

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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASP151

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
ATYR406

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AARG118
AARG152
AGLU276
AARG292
AARG371

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319
ChainResidueDetails
AASP293
AGLY297
AASP324
AASN347

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319
ChainResidueDetails
AASN86
AASN146
AASN200

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AASP151
AGLU277

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AGLU277
AASP151
AARG220
ATRP412
AARG371

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

227561

PDB entries from 2024-11-20

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