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6WCQ

Structure of a substrate-bound DQC ubiquitin ligase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0008013molecular_functionbeta-catenin binding
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0019904molecular_functionprotein domain specific binding
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031467cellular_componentCul7-RING ubiquitin ligase complex
A0031519cellular_componentPcG protein complex
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0051457biological_processmaintenance of protein location in nucleus
A0070936biological_processprotein K48-linked ubiquitination
A0097602molecular_functioncullin family protein binding
A0140677molecular_functionmolecular function activator activity
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1904668biological_processpositive regulation of ubiquitin protein ligase activity
A1990444molecular_functionF-box domain binding
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
C0001701biological_processin utero embryonic development
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005829cellular_componentcytosol
C0005884cellular_componentactin filament
C0006355biological_processregulation of DNA-templated transcription
C0006511biological_processubiquitin-dependent protein catabolic process
C0010506biological_processregulation of autophagy
C0016234cellular_componentinclusion body
C0016567biological_processprotein ubiquitination
C0030496cellular_componentmidbody
C0031463cellular_componentCul3-RING ubiquitin ligase complex
C0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
C0032991cellular_componentprotein-containing complex
C0034451cellular_componentcentriolar satellite
C0034599biological_processcellular response to oxidative stress
C0042802molecular_functionidentical protein binding
C0043433biological_processnegative regulation of DNA-binding transcription factor activity
C0045604biological_processregulation of epidermal cell differentiation
C0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
C0071353biological_processcellular response to interleukin-4
C0097718molecular_functiondisordered domain specific binding
C1902883biological_processnegative regulation of response to oxidative stress
C1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
D0006511biological_processubiquitin-dependent protein catabolic process
D0031625molecular_functionubiquitin protein ligase binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315
ChainResidueDetails
DARG63

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Sensor for electrophilic agents => ECO:0000269|PubMed:29590092
ChainResidueDetails
CCYS257
CCYS273
CCYS288

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Sensor for electrophilic agents => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
CCYS434

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: S-(2-succinyl)cysteine => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
CCYS38
CCYS241
CCYS319
CCYS613

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
CCYS151

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-(2,3-dicarboxypropyl)cysteine => ECO:0000269|PubMed:29590092
ChainResidueDetails
CCYS257
CCYS273

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: S-(2-succinyl)cysteine; alternate => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
CCYS288

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: S-cGMP-cysteine => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
CCYS434

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Arg-Cys) (interchain with C-151 in KEAP1) => ECO:0000269|PubMed:30323285
ChainResidueDetails
CARG135

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Cys-Arg) (interchain with R-135 in KEAP1) => ECO:0000269|PubMed:30323285
ChainResidueDetails
CCYS151

220113

PDB entries from 2024-05-22

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