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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8Q7H

Structure of CUL9-RBX1 ubiquitin E3 ligase complex in unneddylated and neddylated conformation - focused cullin dimer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000226biological_processmicrotubule cytoskeleton organization
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0007088biological_processregulation of mitotic nuclear division
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
B0000166molecular_functionnucleotide binding
B0000226biological_processmicrotubule cytoskeleton organization
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0007088biological_processregulation of mitotic nuclear division
B0008270molecular_functionzinc ion binding
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0031461cellular_componentcullin-RING ubiquitin ligase complex
B0031625molecular_functionubiquitin protein ligase binding
B0046872molecular_functionmetal ion binding
B0061630molecular_functionubiquitin protein ligase activity
C0000165biological_processMAPK cascade
C0000209biological_processprotein polyubiquitination
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0006281biological_processDNA repair
C0006283biological_processtranscription-coupled nucleotide-excision repair
C0006511biological_processubiquitin-dependent protein catabolic process
C0006513biological_processprotein monoubiquitination
C0006974biological_processDNA damage response
C0007283biological_processspermatogenesis
C0008270molecular_functionzinc ion binding
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0019005cellular_componentSCF ubiquitin ligase complex
C0019788molecular_functionNEDD8 transferase activity
C0030163biological_processprotein catabolic process
C0030891cellular_componentVCB complex
C0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
C0031461cellular_componentcullin-RING ubiquitin ligase complex
C0031462cellular_componentCul2-RING ubiquitin ligase complex
C0031463cellular_componentCul3-RING ubiquitin ligase complex
C0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
C0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
C0031466cellular_componentCul5-RING ubiquitin ligase complex
C0031467cellular_componentCul7-RING ubiquitin ligase complex
C0031625molecular_functionubiquitin protein ligase binding
C0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
C0032480biological_processnegative regulation of type I interferon production
C0034450molecular_functionubiquitin-ubiquitin ligase activity
C0034599biological_processcellular response to oxidative stress
C0034644biological_processcellular response to UV
C0042110biological_processT cell activation
C0042770biological_processsignal transduction in response to DNA damage
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0043687biological_processpost-translational protein modification
C0044314biological_processprotein K27-linked ubiquitination
C0044877molecular_functionprotein-containing complex binding
C0045116biological_processprotein neddylation
C0045732biological_processpositive regulation of protein catabolic process
C0046627biological_processnegative regulation of insulin receptor signaling pathway
C0046872molecular_functionmetal ion binding
C0060090molecular_functionmolecular adaptor activity
C0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
C0061630molecular_functionubiquitin protein ligase activity
C0061663molecular_functionNEDD8 ligase activity
C0062197biological_processcellular response to chemical stress
C0070936biological_processprotein K48-linked ubiquitination
C0071230biological_processcellular response to amino acid stimulus
C0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
C0090090biological_processnegative regulation of canonical Wnt signaling pathway
C0090734cellular_componentsite of DNA damage
C0097602molecular_functioncullin family protein binding
C0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
C0160240biological_processRNA polymerase II transcription initiation surveillance
C0160276biological_processnegative regulation of beige fat cell differentiation
C1900076biological_processregulation of cellular response to insulin stimulus
C1901525biological_processnegative regulation of mitophagy
C1902499biological_processpositive regulation of protein autoubiquitination
C1902883biological_processnegative regulation of response to oxidative stress
C1904263biological_processpositive regulation of TORC1 signaling
D0000165biological_processMAPK cascade
D0000209biological_processprotein polyubiquitination
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005829cellular_componentcytosol
D0006281biological_processDNA repair
D0006283biological_processtranscription-coupled nucleotide-excision repair
D0006511biological_processubiquitin-dependent protein catabolic process
D0006513biological_processprotein monoubiquitination
D0006974biological_processDNA damage response
D0007283biological_processspermatogenesis
D0008270molecular_functionzinc ion binding
D0016567biological_processprotein ubiquitination
D0016740molecular_functiontransferase activity
D0019005cellular_componentSCF ubiquitin ligase complex
D0019788molecular_functionNEDD8 transferase activity
D0030163biological_processprotein catabolic process
D0030891cellular_componentVCB complex
D0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
D0031461cellular_componentcullin-RING ubiquitin ligase complex
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0031463cellular_componentCul3-RING ubiquitin ligase complex
D0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
D0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
D0031466cellular_componentCul5-RING ubiquitin ligase complex
D0031467cellular_componentCul7-RING ubiquitin ligase complex
D0031625molecular_functionubiquitin protein ligase binding
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0032480biological_processnegative regulation of type I interferon production
D0034450molecular_functionubiquitin-ubiquitin ligase activity
D0034599biological_processcellular response to oxidative stress
D0034644biological_processcellular response to UV
D0042110biological_processT cell activation
D0042770biological_processsignal transduction in response to DNA damage
D0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
D0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0043687biological_processpost-translational protein modification
D0044314biological_processprotein K27-linked ubiquitination
D0044877molecular_functionprotein-containing complex binding
D0045116biological_processprotein neddylation
D0045732biological_processpositive regulation of protein catabolic process
D0046627biological_processnegative regulation of insulin receptor signaling pathway
D0046872molecular_functionmetal ion binding
D0060090molecular_functionmolecular adaptor activity
D0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
D0061630molecular_functionubiquitin protein ligase activity
D0061663molecular_functionNEDD8 ligase activity
D0062197biological_processcellular response to chemical stress
D0070936biological_processprotein K48-linked ubiquitination
D0071230biological_processcellular response to amino acid stimulus
D0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
D0090090biological_processnegative regulation of canonical Wnt signaling pathway
D0090734cellular_componentsite of DNA damage
D0097602molecular_functioncullin family protein binding
D0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
D0160240biological_processRNA polymerase II transcription initiation surveillance
D0160276biological_processnegative regulation of beige fat cell differentiation
D1900076biological_processregulation of cellular response to insulin stimulus
D1901525biological_processnegative regulation of mitophagy
D1902499biological_processpositive regulation of protein autoubiquitination
D1902883biological_processnegative regulation of response to oxidative stress
D1904263biological_processpositive regulation of TORC1 signaling
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005737cellular_componentcytoplasm
N0005829cellular_componentcytosol
N0006357biological_processregulation of transcription by RNA polymerase II
N0006508biological_processproteolysis
N0006511biological_processubiquitin-dependent protein catabolic process
N0008104biological_processintracellular protein localization
N0009653biological_processanatomical structure morphogenesis
N0016567biological_processprotein ubiquitination
N0019941biological_processmodification-dependent protein catabolic process
N0030162biological_processregulation of proteolysis
N0031386molecular_functionprotein tag activity
N0031625molecular_functionubiquitin protein ligase binding
N0036211biological_processprotein modification process
N0045116biological_processprotein neddylation
N0070062cellular_componentextracellular exosome
N0072757biological_processcellular response to camptothecin
N0098794cellular_componentpostsynapse
N0098978cellular_componentglutamatergic synapse
N0150052biological_processregulation of postsynapse assembly
Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgDSTSCIG
ChainResidueDetails
APHE1237-GLY1246
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
ChainResidueDetails
NLYS27-ASP52
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CnHgFCwrCL
ChainResidueDetails
ACYS2257-LEU2266
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. VLscIlhLLGQgYVkRrddrpqiLmYaA
ChainResidueDetails
AVAL1926-ALA1953
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DPL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DPL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsRegion: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"(Microbial infection) Deamidated glutamine","evidences":[{"source":"PubMed","id":"20688984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23175788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23589306","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26632597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PubMed","id":"38316879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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