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5BO9

Structure of human sialyltransferase ST8SiaIII in complex with CMP-3FNeu5Ac and Sia-6S-LacNAc

Functional Information from GO Data
ChainGOidnamespacecontents
A0006486biological_processprotein glycosylation
A0008373molecular_functionsialyltransferase activity
B0006486biological_processprotein glycosylation
B0008373molecular_functionsialyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:26192331
ChainResidueDetails
AHIS354
BHIS354

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305|PubMed:26192331, ECO:0007744|PDB:5BO9
ChainResidueDetails
ASER300
BASN167
BASN190
BSER300
BTHR301
BGLY302
BTRP322
BTYR336
BHIS337
AASN190
ATHR301
AGLY302
ATRP322
ATYR336
AHIS337
AASN167

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26192331, ECO:0000269|Ref.7, ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO8, ECO:0007744|PDB:5BO9, ECO:0007744|PDB:5CXY
ChainResidueDetails
AASN93
BASN93

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26192331, ECO:0007744|PDB:5BO9
ChainResidueDetails
AASN113
BASN113

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26192331, ECO:0000269|Ref.7, ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7, ECO:0007744|PDB:5BO9, ECO:0007744|PDB:5CXY
ChainResidueDetails
AASN160
BASN160

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26192331, ECO:0007744|PDB:5BO6, ECO:0007744|PDB:5BO7, ECO:0007744|PDB:5BO8, ECO:0007744|PDB:5BO9, ECO:0007744|PDB:5CXY
ChainResidueDetails
AASN206
BASN206

219869

PDB entries from 2024-05-15

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