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

1ING

INFLUENZA A SUBTYPE N2 NEURAMINIDASE COMPLEXED WITH AROMATIC BANA109 INHIBITOR

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_idCAA
Number of Residues11
DetailsSUBSTRATE (SIALIC ACID) BINDING RESIDUES CATALYTIC SITE IN CHAIN A
ChainResidue
AARG118
AARG371
ATYR406
AGLU119
AASP151
AARG152
ATRP178
AILE222
AARG224
AGLU276
AARG292

site_idCAB
Number of Residues11
DetailsSUBSTRATE (SIALIC ACID) BINDING RESIDUES CATALYTIC SITE IN CHAIN B
ChainResidue
BARG118
BGLU119
BASP151
BARG152
BTRP178
BILE222
BARG224
BGLU276
BARG292
BARG371
BTYR406

Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CsCypRypGVrC
ChainResidueDetails
ACYS278-CYS289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASP151
BASP151

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
ATYR406
BTYR406

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AARG118
BARG371
AARG152
AGLU276
AARG292
AARG371
BARG118
BARG152
BGLU276
BARG292

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809
ChainResidueDetails
AASP293
BTHR346
AGLY297
AASP324
AGLY345
ATHR346
BASP293
BGLY297
BASP324
BGLY345

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809
ChainResidueDetails
AGLN347
BGLN347

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809
ChainResidueDetails
AASN86
BASN86

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809
ChainResidueDetails
AASN146
AASN200
BASN146
BASN200

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809
ChainResidueDetails
AASN234
BASN234

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASN402
BASN402

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a4g
ChainResidueDetails
BASP151
BGLU277

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon