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1A4Q

INFLUENZA VIRUS B/BEIJING/1/87 NEURAMINIDASE COMPLEXED WITH DIHYDROPYRAN-PHENETHYL-PROPYL-CARBOXAMIDE

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
Functional Information from PDB Data
site_idCHA
Number of Residues5
DetailsHIGH AFFINITY CALCIUM BINDING SITE IN CHAIN A.
ChainResidue
AASP323
AGLY343
AGLY345
ATHR296
AASP292

site_idCHB
Number of Residues5
DetailsHIGH AFFINITY CALCIUM BINDING SITE IN CHAIN B.
ChainResidue
BASP323
BGLY343
BGLY345
BTHR296
BASP292

site_idCLA
Number of Residues1
DetailsLOW AFFINITY CALCIUM BINDING SITE IN CHAIN A.
ChainResidue
AGLU167

site_idCLB
Number of Residues1
DetailsLOW AFFINITY CALCIUM BINDING SITE IN CHAIN B.
ChainResidue
BGLU167

site_idLIA
Number of Residues10
DetailsBINDING SITE FOR INHIBITOR IN CHAIN A.
ChainResidue
AARG149
AILE220
AARG222
ATRP176
AGLU274
AASP148
ATYR408
AASP323
AARG115
AARG291

site_idLIB
Number of Residues10
DetailsBINDING SITE FOR INHIBITOR IN CHAIN B.
ChainResidue
BASP323
BARG115
BARG291
BARG149
BILE220
BARG222
BTRP176
BGLU274
BASP148
BTYR408

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASP148
BASP148

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
ATYR408
BTYR408

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AARG115
BARG373
AARG149
AGLU274
AARG291
AARG373
BARG115
BARG149
BGLU274
BARG291

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1740114
ChainResidueDetails
AASP292
AASP323
BASP292
BASP323

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:1740114
ChainResidueDetails
ATHR296
AGLY343
AGLY345
BTHR296
BGLY343
BGLY345

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASN143
BASN143

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1740114
ChainResidueDetails
AASN283
BASN283

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
AASP148
AGLU275

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
BASP148
BGLU275

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PDB entries from 2024-11-06

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