Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8E6J

3H03 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
A0033644cellular_componenthost cell membrane
A0046761biological_processviral budding from plasma membrane
A0055036cellular_componentvirion membrane
B0004308molecular_functionexo-alpha-sialidase activity
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0033644cellular_componenthost cell membrane
B0046761biological_processviral budding from plasma membrane
B0055036cellular_componentvirion membrane
C0004308molecular_functionexo-alpha-sialidase activity
C0005975biological_processcarbohydrate metabolic process
C0016020cellular_componentmembrane
C0033644cellular_componenthost cell membrane
C0046761biological_processviral budding from plasma membrane
C0055036cellular_componentvirion membrane
D0004308molecular_functionexo-alpha-sialidase activity
D0005975biological_processcarbohydrate metabolic process
D0016020cellular_componentmembrane
D0033644cellular_componenthost cell membrane
D0046761biological_processviral budding from plasma membrane
D0055036cellular_componentvirion membrane
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR192-HIS198
HTYR194-HIS200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASP151
BASP151
CASP151
DASP151

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
ATYR406
BTYR406
CTYR406
DTYR406

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AARG118
AARG152
AGLU276
AARG292
AARG371
BARG118
BARG152
BGLU276
BARG292
BARG371
CARG118
CARG152
CGLU276
CARG292
CARG371
DARG118
DARG152
DGLU276
DARG292
DARG371

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:18715929
ChainResidueDetails
AASP293
AGLY297
AASP324
AASN347
BASP293
BGLY297
BASP324
BASN347
CASP293
CGLY297
CASP324
CASN347
DASP293
DGLY297
DASP324
DASN347

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASN88
AASN234
BASN88
BASN234
CASN88
CASN234
DASN88
DASN234

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:18715929
ChainResidueDetails
AASN146
BASN146
CASN146
DASN146

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon