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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6C26

The Cryo-EM structure of a eukaryotic oligosaccharyl transferase complex

Functional Information from GO Data
ChainGOidnamespacecontents
10009101biological_processglycoprotein biosynthetic process
10016020cellular_componentmembrane
20003674molecular_functionmolecular_function
20005515molecular_functionprotein binding
20005783cellular_componentendoplasmic reticulum
20005789cellular_componentendoplasmic reticulum membrane
20006486biological_processobsolete protein glycosylation
20006487biological_processprotein N-linked glycosylation
20008250cellular_componentoligosaccharyltransferase complex
20016020cellular_componentmembrane
40005515molecular_functionprotein binding
40005739cellular_componentmitochondrion
40005789cellular_componentendoplasmic reticulum membrane
40006486biological_processobsolete protein glycosylation
40006487biological_processprotein N-linked glycosylation
40008250cellular_componentoligosaccharyltransferase complex
40030674molecular_functionprotein-macromolecule adaptor activity
50005198molecular_functionstructural molecule activity
50005789cellular_componentendoplasmic reticulum membrane
50006486biological_processobsolete protein glycosylation
50006487biological_processprotein N-linked glycosylation
50008250cellular_componentoligosaccharyltransferase complex
A0004576molecular_functionoligosaccharyl transferase activity
A0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006486biological_processobsolete protein glycosylation
A0006487biological_processprotein N-linked glycosylation
A0008250cellular_componentoligosaccharyltransferase complex
A0009101biological_processglycoprotein biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
B0005789cellular_componentendoplasmic reticulum membrane
B0018279biological_processprotein N-linked glycosylation via asparagine
C0008250cellular_componentoligosaccharyltransferase complex
C0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues230
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues111
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues11
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsRegion: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues24
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsMotif: {"description":"DXD motif 1","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsMotif: {"description":"DXD motif 2","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsMotif: {"description":"WWDYG motif","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues7
DetailsMotif: {"description":"DK motif","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsSite: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues28
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues25
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues18
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"12810948","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues373
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues35
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2025-12-31

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