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2F10

Crystal Structure of the Human Sialidase Neu2 in Complex with Peramivir inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0006516biological_processglycoprotein catabolic process
A0006689biological_processganglioside catabolic process
A0009313biological_processoligosaccharide catabolic process
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046479biological_processglycosphingolipid catabolic process
A0052794molecular_functionexo-alpha-(2->3)-sialidase activity
A0052795molecular_functionexo-alpha-(2->6)-sialidase activity
A0052796molecular_functionexo-alpha-(2->8)-sialidase activity
A1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 381
ChainResidue
AGLN14
AALA17
AHIS18
ATYR20

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCZ A 382
ChainResidue
AGLU218
AARG237
AARG304
ATYR334
AARG21
AGLU39
AARG41
AASN86
ATYR179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:22228546
ChainResidueDetails
AASP46

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ATYR334

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AGLU355

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AARG21
AARG41
ATYR179
ATYR181
AGLU218
AARG237
AARG304

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1euu
ChainResidueDetails
ATYR334
AGLU218

221371

PDB entries from 2024-06-19

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