Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8KEV

Cryo-EM structure of HRD1-SEL1L-XTP3B (state D1) complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000836cellular_componentHrd1p ubiquitin ligase complex
A0000839cellular_componentHrd1p ubiquitin ligase ERAD-L complex
A0002327biological_processimmature B cell differentiation
A0002826biological_processnegative regulation of T-helper 1 type immune response
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005790cellular_componentsmooth endoplasmic reticulum
A0006511biological_processubiquitin-dependent protein catabolic process
A0008270molecular_functionzinc ion binding
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0030970biological_processretrograde protein transport, ER to cytosol
A0036503biological_processERAD pathway
A0036513cellular_componentDerlin-1 retrotranslocation complex
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0044322cellular_componentendoplasmic reticulum quality control compartment
A0046872molecular_functionmetal ion binding
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0051087molecular_functionprotein-folding chaperone binding
A0051117molecular_functionATPase binding
A0061630molecular_functionubiquitin protein ligase activity
A0070936biological_processprotein K48-linked ubiquitination
A0140297molecular_functionDNA-binding transcription factor binding
A1902236biological_processnegative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
A1904380biological_processendoplasmic reticulum mannose trimming
A1990381molecular_functionubiquitin-specific protease binding
B0000836cellular_componentHrd1p ubiquitin ligase complex
B0000839cellular_componentHrd1p ubiquitin ligase ERAD-L complex
B0002327biological_processimmature B cell differentiation
B0002826biological_processnegative regulation of T-helper 1 type immune response
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005790cellular_componentsmooth endoplasmic reticulum
B0006511biological_processubiquitin-dependent protein catabolic process
B0008270molecular_functionzinc ion binding
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0030970biological_processretrograde protein transport, ER to cytosol
B0036503biological_processERAD pathway
B0036513cellular_componentDerlin-1 retrotranslocation complex
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044322cellular_componentendoplasmic reticulum quality control compartment
B0046872molecular_functionmetal ion binding
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0051087molecular_functionprotein-folding chaperone binding
B0051117molecular_functionATPase binding
B0061630molecular_functionubiquitin protein ligase activity
B0070936biological_processprotein K48-linked ubiquitination
B0140297molecular_functionDNA-binding transcription factor binding
B1902236biological_processnegative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
B1904380biological_processendoplasmic reticulum mannose trimming
B1990381molecular_functionubiquitin-specific protease binding
Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. ChfPFlFldkeydeCtsdgredgrlWCattyDYkadekWgFC
ChainResidueDetails
DCYS127-CYS168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues832
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-THR4
ALYS63-ASP98
ASER162-SER169
AARG246-HIS617
BMET1-THR4
BLYS63-ASP98
BSER162-SER169
BARG246-HIS617

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AALA5-LEU25
BILE141-HIS161
BVAL170-ILE190
BLEU225-ILE245
ASER42-GLY62
APHE99-LEU119
AILE141-HIS161
AVAL170-ILE190
ALEU225-ILE245
BALA5-LEU25
BSER42-GLY62
BPHE99-LEU119

site_idSWS_FT_FI3
Number of Residues136
DetailsTOPO_DOM: Lumenal => ECO:0000305
ChainResidueDetails
ALYS26-PRO41
AALA120-ARG140
ALYS191-VAL224
BLYS26-PRO41
BALA120-ARG140
BLYS191-VAL224

site_idSWS_FT_FI4
Number of Residues78
DetailsZN_FING: RING-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS291-ARG330
BCYS291-ARG330

site_idSWS_FT_FI5
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:30345569, ECO:0007744|PDB:6A3Z
ChainResidueDetails
ACYS291
BCYS294
BCYS307
BHIS309
BHIS312
BCYS315
BCYS326
BCYS329
ACYS294
ACYS307
AHIS309
AHIS312
ACYS315
ACYS326
ACYS329
BCYS291

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER613
BSER613

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
DASN431
DASN608
CASN431
CASN608

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon