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6LXI

Crystal structure of Z2B3 Fab in complex with influenza virus neuraminidase from A/Brevig Mission/1/1918 (H1N1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0020002cellular_componenthost cell plasma membrane
A0033644cellular_componenthost cell membrane
A0044423cellular_componentvirion component
A0046761biological_processviral budding from plasma membrane
A0046872molecular_functionmetal ion binding
A0055036cellular_componentvirion membrane
B0004308molecular_functionexo-alpha-sialidase activity
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0020002cellular_componenthost cell plasma membrane
B0033644cellular_componenthost cell membrane
B0044423cellular_componentvirion component
B0046761biological_processviral budding from plasma membrane
B0046872molecular_functionmetal ion binding
B0055036cellular_componentvirion membrane
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
HTYR213-HIS219
LTYR195-HIS201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsTOPO_DOM: Intravirion => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AMET1-LYS6
BMET1-LYS6

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AILE7-GLY27
BILE7-GLY27

site_idSWS_FT_FI3
Number of Residues882
DetailsTOPO_DOM: Virion surface => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASN28-LYS469
BASN28-LYS469

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASP151
BASP151

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
ATYR402
BTYR402

site_idSWS_FT_FI6
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AARG118
BARG368
AARG152
AGLU277
AARG293
AARG368
BARG118
BARG152
BGLU277
BARG293

site_idSWS_FT_FI7
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:18715929
ChainResidueDetails
AASP294
AGLY298
AASP324
AASN344
BASP294
BGLY298
BASP324
BASN344

site_idSWS_FT_FI8
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASN50
BASN68
BASN88
BASN235
AASN58
AASN63
AASN68
AASN88
AASN235
BASN50
BASN58
BASN63

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:18715929
ChainResidueDetails
AASN146
BASN146

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PDB entries from 2025-05-21

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