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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8B6L

Subtomogram average of the human Sec61-TRAP-OSTA-translocon

Functional Information from GO Data
ChainGOidnamespacecontents
A0005048molecular_functionsignal sequence binding
A0005262molecular_functioncalcium channel activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005784cellular_componentSec61 translocon complex
A0005789cellular_componentendoplasmic reticulum membrane
A0006613biological_processcotranslational protein targeting to membrane
A0006614biological_processSRP-dependent cotranslational protein targeting to membrane
A0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
A0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
A0007029biological_processendoplasmic reticulum organization
A0008320molecular_functionprotein transmembrane transporter activity
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0031204biological_processpost-translational protein targeting to membrane, translocation
A0034341biological_processresponse to type II interferon
A0039019biological_processpronephric nephron development
A0043022molecular_functionribosome binding
A0045047biological_processprotein targeting to ER
A0045048biological_processprotein insertion into ER membrane
A0070588biological_processcalcium ion transmembrane transport
B0003723molecular_functionRNA binding
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005784cellular_componentSec61 translocon complex
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
B0006886biological_processintracellular protein transport
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0030970biological_processretrograde protein transport, ER to cytosol
B0031204biological_processpost-translational protein targeting to membrane, translocation
B0031205cellular_componentendoplasmic reticulum Sec complex
B0036503biological_processERAD pathway
B0043022molecular_functionribosome binding
B0044322cellular_componentendoplasmic reticulum quality control compartment
B0048408molecular_functionepidermal growth factor binding
C0005515molecular_functionprotein binding
C0005784cellular_componentSec61 translocon complex
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0006605biological_processprotein targeting
C0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
C0006886biological_processintracellular protein transport
C0008320molecular_functionprotein transmembrane transporter activity
C0015031biological_processprotein transport
C0016020cellular_componentmembrane
C0031204biological_processpost-translational protein targeting to membrane, translocation
C0043022molecular_functionribosome binding
C0045047biological_processprotein targeting to ER
C0071261cellular_componentSsh1 translocon complex
E0005789cellular_componentendoplasmic reticulum membrane
F0005783cellular_componentendoplasmic reticulum
F0016020cellular_componentmembrane
G0005515molecular_functionprotein binding
G0005783cellular_componentendoplasmic reticulum
G0005789cellular_componentendoplasmic reticulum membrane
G0006614biological_processSRP-dependent cotranslational protein targeting to membrane
G0016020cellular_componentmembrane
G0031204biological_processpost-translational protein targeting to membrane, translocation
H0005783cellular_componentendoplasmic reticulum
H0016020cellular_componentmembrane
I0004576molecular_functionoligosaccharyl transferase activity
I0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
I0005515molecular_functionprotein binding
I0005783cellular_componentendoplasmic reticulum
I0005789cellular_componentendoplasmic reticulum membrane
I0006486biological_processobsolete protein glycosylation
I0006487biological_processprotein N-linked glycosylation
I0008250cellular_componentoligosaccharyltransferase complex
I0009101biological_processglycoprotein biosynthetic process
I0016020cellular_componentmembrane
I0016740molecular_functiontransferase activity
I0016757molecular_functionglycosyltransferase activity
I0043686biological_processobsolete co-translational protein modification
I0043687biological_processpost-translational protein modification
I0046872molecular_functionmetal ion binding
I0160226cellular_componentoligosaccharyltransferase complex A
I0180058biological_processprotein co-translational transfer of dolichol-linked oligosaccharide
J0004579molecular_functiondolichyl-diphosphooligosaccharide-protein glycotransferase activity
J0005515molecular_functionprotein binding
J0005783cellular_componentendoplasmic reticulum
J0005789cellular_componentendoplasmic reticulum membrane
J0006486biological_processobsolete protein glycosylation
J0006487biological_processprotein N-linked glycosylation
J0008250cellular_componentoligosaccharyltransferase complex
J0009101biological_processglycoprotein biosynthetic process
J0016020cellular_componentmembrane
J0030674molecular_functionprotein-macromolecule adaptor activity
J0043686biological_processobsolete co-translational protein modification
J0160226cellular_componentoligosaccharyltransferase complex A
K0005515molecular_functionprotein binding
K0005783cellular_componentendoplasmic reticulum
K0005789cellular_componentendoplasmic reticulum membrane
K0006486biological_processobsolete protein glycosylation
K0006487biological_processprotein N-linked glycosylation
K0008250cellular_componentoligosaccharyltransferase complex
K0160226cellular_componentoligosaccharyltransferase complex A
K0160227cellular_componentoligosaccharyltransferase complex B
L0005515molecular_functionprotein binding
L0005737cellular_componentcytoplasm
L0005783cellular_componentendoplasmic reticulum
L0005789cellular_componentendoplasmic reticulum membrane
L0006486biological_processobsolete protein glycosylation
L0006487biological_processprotein N-linked glycosylation
L0008250cellular_componentoligosaccharyltransferase complex
L0009306biological_processprotein secretion
L0016020cellular_componentmembrane
L0034976biological_processresponse to endoplasmic reticulum stress
L0062062molecular_functionoligosaccharyltransferase complex binding
L0160226cellular_componentoligosaccharyltransferase complex A
L0160227cellular_componentoligosaccharyltransferase complex B
M0005789cellular_componentendoplasmic reticulum membrane
M0006486biological_processobsolete protein glycosylation
M0006487biological_processprotein N-linked glycosylation
M0006915biological_processapoptotic process
M0008047molecular_functionenzyme activator activity
M0008250cellular_componentoligosaccharyltransferase complex
M0009101biological_processglycoprotein biosynthetic process
M0016020cellular_componentmembrane
M0031647biological_processregulation of protein stability
M0043066biological_processnegative regulation of apoptotic process
M0160226cellular_componentoligosaccharyltransferase complex A
M0160227cellular_componentoligosaccharyltransferase complex B
N0005789cellular_componentendoplasmic reticulum membrane
N0018279biological_processprotein N-linked glycosylation via asparagine
O0009101biological_processglycoprotein biosynthetic process
O0016020cellular_componentmembrane
P0008250cellular_componentoligosaccharyltransferase complex
P0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00755
Number of Residues20
DetailsSECY_1 Protein secY signature 1. TLMeLGIsPIVtSGLIMQLL
ChainResidueDetails
ATHR75-LEU94
site_idPS00756
Number of Residues19
DetailsSECY_2 Protein secY signature 2. LLdElLQkgyGLGSGiSLF
ChainResidueDetails
ALEU164-PHE182
site_idPS01067
Number of Residues29
DetailsSECE_SEC61G Protein secE/sec61-gamma signature. FvKDsIrlVkRctKPdrkEfqkiaMATAI
ChainResidueDetails
CPHE14-ILE42
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues317
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues602
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues445
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues35
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues369
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues206
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues23
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
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_FI14
Number of Residues2
DetailsMotif: {"description":"DXD motif 1","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsMotif: {"description":"DXD motif 2","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues3
DetailsMotif: {"description":"SVSE motif","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsMotif: {"description":"WWDYG motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues7
DetailsMotif: {"description":"DK motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
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_FI21
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YQ5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
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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