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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9YGY

Structure of a GRP94 folding intermediate engaged with a CCDC134- and FKBP11-bound secretory translocon

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
70005515molecular_functionprotein binding
70005783cellular_componentendoplasmic reticulum
70005789cellular_componentendoplasmic reticulum membrane
70031204biological_processpost-translational protein targeting to membrane, translocation
D0005048molecular_functionsignal sequence binding
D0005262molecular_functioncalcium channel activity
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0005784cellular_componentSec61 translocon complex
D0005789cellular_componentendoplasmic reticulum membrane
D0006613biological_processcotranslational protein targeting to membrane
D0006614biological_processSRP-dependent cotranslational protein targeting to membrane
D0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
D0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
D0007029biological_processendoplasmic reticulum organization
D0008320molecular_functionprotein transmembrane transporter activity
D0015031biological_processprotein transport
D0016020cellular_componentmembrane
D0031204biological_processpost-translational protein targeting to membrane, translocation
D0034341biological_processresponse to type II interferon
D0039019biological_processpronephric nephron development
D0043022molecular_functionribosome binding
D0045047biological_processprotein targeting to ER
D0045048biological_processprotein insertion into ER membrane
D0070588biological_processcalcium ion transmembrane transport
E0003723molecular_functionRNA binding
E0005085molecular_functionguanyl-nucleotide exchange factor activity
E0005515molecular_functionprotein binding
E0005783cellular_componentendoplasmic reticulum
E0005784cellular_componentSec61 translocon complex
E0005789cellular_componentendoplasmic reticulum membrane
E0005829cellular_componentcytosol
E0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
E0015031biological_processprotein transport
E0016020cellular_componentmembrane
E0030970biological_processretrograde protein transport, ER to cytosol
E0031204biological_processpost-translational protein targeting to membrane, translocation
E0031205cellular_componentendoplasmic reticulum Sec complex
E0036503biological_processERAD pathway
E0043022molecular_functionribosome binding
E0044322cellular_componentendoplasmic reticulum quality control compartment
E0048408molecular_functionepidermal growth factor binding
F0005515molecular_functionprotein binding
F0005784cellular_componentSec61 translocon complex
F0005789cellular_componentendoplasmic reticulum membrane
F0005829cellular_componentcytosol
F0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
F0008320molecular_functionprotein transmembrane transporter activity
F0015031biological_processprotein transport
F0016020cellular_componentmembrane
F0031204biological_processpost-translational protein targeting to membrane, translocation
F0043022molecular_functionribosome binding
F0045047biological_processprotein targeting to ER
F0071261cellular_componentSsh1 translocon complex
G0005783cellular_componentendoplasmic reticulum
G0005789cellular_componentendoplasmic reticulum membrane
G0005829cellular_componentcytosol
G0005840cellular_componentribosome
G0005881cellular_componentcytoplasmic microtubule
G0006986biological_processresponse to unfolded protein
G0007009biological_processplasma membrane organization
G0009101biological_processglycoprotein biosynthetic process
G0015031biological_processprotein transport
G0016020cellular_componentmembrane
G0030968biological_processendoplasmic reticulum unfolded protein response
G0036211biological_processprotein modification process
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
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
J0016020cellular_componentmembrane
J0030674molecular_functionprotein-macromolecule adaptor activity
J0043686biological_processobsolete co-translational protein modification
J0160226cellular_componentoligosaccharyltransferase complex A
K20005515molecular_functionprotein binding
K20005783cellular_componentendoplasmic reticulum
K20005789cellular_componentendoplasmic reticulum membrane
K20006486biological_processobsolete protein glycosylation
K20006487biological_processprotein N-linked glycosylation
K20008250cellular_componentoligosaccharyltransferase complex
K20160226cellular_componentoligosaccharyltransferase complex A
K20160227cellular_componentoligosaccharyltransferase complex B
L20005515molecular_functionprotein binding
L20005737cellular_componentcytoplasm
L20005783cellular_componentendoplasmic reticulum
L20005789cellular_componentendoplasmic reticulum membrane
L20006486biological_processobsolete protein glycosylation
L20006487biological_processprotein N-linked glycosylation
L20008250cellular_componentoligosaccharyltransferase complex
L20009306biological_processprotein secretion
L20016020cellular_componentmembrane
L20034976biological_processresponse to endoplasmic reticulum stress
L20062062molecular_functionoligosaccharyltransferase complex binding
L20160226cellular_componentoligosaccharyltransferase complex A
L20160227cellular_componentoligosaccharyltransferase complex B
M20005789cellular_componentendoplasmic reticulum membrane
M20006486biological_processobsolete protein glycosylation
M20006487biological_processprotein N-linked glycosylation
M20006915biological_processapoptotic process
M20008047molecular_functionenzyme activator activity
M20008250cellular_componentoligosaccharyltransferase complex
M20009101biological_processglycoprotein biosynthetic process
M20016020cellular_componentmembrane
M20031647biological_processregulation of protein stability
M20043066biological_processnegative regulation of apoptotic process
M20160226cellular_componentoligosaccharyltransferase complex A
M20160227cellular_componentoligosaccharyltransferase complex B
N0005783cellular_componentendoplasmic reticulum
N0005789cellular_componentendoplasmic reticulum membrane
N0006486biological_processobsolete protein glycosylation
N0006487biological_processprotein N-linked glycosylation
N0008047molecular_functionenzyme activator activity
N0008250cellular_componentoligosaccharyltransferase complex
N0030674molecular_functionprotein-macromolecule adaptor activity
N0160226cellular_componentoligosaccharyltransferase complex A
Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE
ChainResidueDetails
y3TYR94-GLU103
site_idPS00755
Number of Residues20
DetailsSECY_1 Protein secY signature 1. TLMeLGIsPIVtSGLIMQLL
ChainResidueDetails
DTHR75-LEU94
site_idPS00756
Number of Residues19
DetailsSECY_2 Protein secY signature 2. LLdElLQkgyGLGSGiSLF
ChainResidueDetails
DLEU164-PHE182
site_idPS01067
Number of Residues29
DetailsSECE_SEC61G Protein secE/sec61-gamma signature. FvKDsIrlVkRctKPdrkEfqkiaMATAI
ChainResidueDetails
FPHE14-ILE42
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_FI3
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues773
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues789
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues416
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DCF9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
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 Residues87
DetailsDomain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues22
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsMotif: {"description":"Prevents secretion from ER","evidences":[{"source":"PubMed","id":"39509507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues7
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00768","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22644376","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"38670073","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues142
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
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_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues206
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues47
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI20
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_FI21
Number of Residues2
DetailsMotif: {"description":"DXD motif 1","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsMotif: {"description":"DXD motif 2","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues3
DetailsMotif: {"description":"SVSE motif","evidences":[{"source":"UniProtKB","id":"Q5HTX9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsMotif: {"description":"WWDYG motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues7
DetailsMotif: {"description":"DK motif","evidences":[{"source":"UniProtKB","id":"P39007","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
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_FI28
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"B9KDD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues39
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
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_FI32
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YQ5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
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
site_idSWS_FT_FI35
Number of Residues2
DetailsMotif: {"description":"SRT pseudosubstrate motif","evidences":[{"source":"PubMed","id":"39509507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P41148","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31296534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39509507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31296534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39509507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31296534","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39509507","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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