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3APO

Crystal structure of full-length ERdj5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001671molecular_functionATPase activator activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0016491molecular_functionoxidoreductase activity
A0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
A0019153molecular_functionprotein-disulfide reductase (glutathione) activity
A0030544molecular_functionHsp70 protein binding
A0034663cellular_componentendoplasmic reticulum chaperone complex
A0034975biological_processprotein folding in endoplasmic reticulum
A0034976biological_processresponse to endoplasmic reticulum stress
A0036498biological_processIRE1-mediated unfolded protein response
A0036503biological_processERAD pathway
A0051087molecular_functionprotein-folding chaperone binding
A0051117molecular_functionATPase binding
A0051787molecular_functionmisfolded protein binding
A0070059biological_processintrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. KDEL
ChainResidueDetails
ALYS790-LEU793

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues99
DetailsDomain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsDomain: {"description":"Thioredoxin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues105
DetailsDomain: {"description":"Thioredoxin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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