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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8AGC

Structure of yeast oligosaccharylransferase complex with lipid-linked oligosaccharide and non-acceptor peptide bound

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0018279biological_processprotein N-linked glycosylation via asparagine
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005789cellular_componentendoplasmic reticulum membrane
B0006486biological_processobsolete protein glycosylation
B0006487biological_processprotein N-linked glycosylation
B0008250cellular_componentoligosaccharyltransferase complex
B0030674molecular_functionprotein-macromolecule adaptor activity
C0005198molecular_functionstructural molecule activity
C0005789cellular_componentendoplasmic reticulum membrane
C0006486biological_processobsolete protein glycosylation
C0006487biological_processprotein N-linked glycosylation
C0008250cellular_componentoligosaccharyltransferase complex
D0003674molecular_functionmolecular_function
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006486biological_processobsolete protein glycosylation
D0006487biological_processprotein N-linked glycosylation
D0008250cellular_componentoligosaccharyltransferase complex
D0016020cellular_componentmembrane
E0006486biological_processobsolete protein glycosylation
E0016020cellular_componentmembrane
F0008250cellular_componentoligosaccharyltransferase complex
F0016020cellular_componentmembrane
G0005789cellular_componentendoplasmic reticulum membrane
G0018279biological_processprotein N-linked glycosylation via asparagine
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 Residues143
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29466327","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues21
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
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_FI6
Number of Residues24
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsMotif: {"description":"DXD motif 1","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsMotif: {"description":"DXD motif 2","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues3
DetailsMotif: {"description":"SVSE motif","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsMotif: {"description":"WWDYG motif","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsMotif: {"description":"DK motif","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsSite: {"description":"Interacts with target acceptor peptide in protein substrate","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues8
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"12810948","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues18
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"12810948","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues33
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues260
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues23
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29301962","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues23
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues36
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2025-10-29

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