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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6S7O

Cryo-EM structure of human oligosaccharyltransferase complex OST-A

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
A0009101biological_processglycoprotein biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0043686biological_processobsolete co-translational protein modification
A0043687biological_processpost-translational protein modification
A0046872molecular_functionmetal ion binding
A0160226cellular_componentoligosaccharyltransferase complex A
A0180058biological_processprotein co-translational transfer of dolichol-linked oligosaccharide
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006486biological_processobsolete protein glycosylation
B0006487biological_processprotein N-linked glycosylation
B0008250cellular_componentoligosaccharyltransferase complex
B0160226cellular_componentoligosaccharyltransferase complex A
B0160227cellular_componentoligosaccharyltransferase complex B
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006486biological_processobsolete protein glycosylation
C0006487biological_processprotein N-linked glycosylation
C0008250cellular_componentoligosaccharyltransferase complex
C0009306biological_processprotein secretion
C0016020cellular_componentmembrane
C0034976biological_processresponse to endoplasmic reticulum stress
C0062062molecular_functionoligosaccharyltransferase complex binding
C0160226cellular_componentoligosaccharyltransferase complex A
C0160227cellular_componentoligosaccharyltransferase complex B
D0005789cellular_componentendoplasmic reticulum membrane
D0006486biological_processobsolete protein glycosylation
D0006487biological_processprotein N-linked glycosylation
D0006915biological_processapoptotic process
D0008047molecular_functionenzyme activator activity
D0008250cellular_componentoligosaccharyltransferase complex
D0009101biological_processglycoprotein biosynthetic process
D0016020cellular_componentmembrane
D0031647biological_processregulation of protein stability
D0043066biological_processnegative regulation of apoptotic process
D0160226cellular_componentoligosaccharyltransferase complex A
D0160227cellular_componentoligosaccharyltransferase complex B
E0009101biological_processglycoprotein biosynthetic process
E0016020cellular_componentmembrane
F0008250cellular_componentoligosaccharyltransferase complex
F0016020cellular_componentmembrane
G0005789cellular_componentendoplasmic reticulum membrane
G0018279biological_processprotein N-linked glycosylation via asparagine
H0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
H0005515molecular_functionprotein binding
H0005783cellular_componentendoplasmic reticulum
H0005789cellular_componentendoplasmic reticulum membrane
H0006486biological_processobsolete protein glycosylation
H0006487biological_processprotein N-linked glycosylation
H0008250cellular_componentoligosaccharyltransferase complex
H0009101biological_processglycoprotein biosynthetic process
H0016020cellular_componentmembrane
H0030674molecular_functionprotein-macromolecule adaptor activity
H0043686biological_processobsolete co-translational protein modification
H0160226cellular_componentoligosaccharyltransferase complex A
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues297
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues138
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues206
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues11
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
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 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":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues3
DetailsMotif: {"description":"SVSE motif","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsMotif: {"description":"WWDYG motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues7
DetailsMotif: {"description":"DK motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
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_FI13
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues391
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues39
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YQ5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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