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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5N4W

Crystal structure of the Cul2-Rbx1-EloBC-VHL ubiquitin ligase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0010498biological_processproteasomal protein catabolic process
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0030163biological_processprotein catabolic process
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0031981cellular_componentnuclear lumen
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0097193biological_processintrinsic apoptotic signaling pathway
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
A0160276biological_processnegative regulation of beige fat cell differentiation
B0006368biological_processtranscription elongation by RNA polymerase II
B0030891cellular_componentVCB complex
B0070449cellular_componentelongin complex
C0006511biological_processubiquitin-dependent protein catabolic process
R0000165biological_processMAPK cascade
R0000209biological_processprotein polyubiquitination
R0004842molecular_functionubiquitin-protein transferase activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005813cellular_componentcentrosome
R0005829cellular_componentcytosol
R0006281biological_processDNA repair
R0006283biological_processtranscription-coupled nucleotide-excision repair
R0006511biological_processubiquitin-dependent protein catabolic process
R0006513biological_processprotein monoubiquitination
R0006974biological_processDNA damage response
R0007283biological_processspermatogenesis
R0008270molecular_functionzinc ion binding
R0016567biological_processprotein ubiquitination
R0016740molecular_functiontransferase activity
R0019005cellular_componentSCF ubiquitin ligase complex
R0019788molecular_functionNEDD8 transferase activity
R0030163biological_processprotein catabolic process
R0030891cellular_componentVCB complex
R0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
R0031461cellular_componentcullin-RING ubiquitin ligase complex
R0031462cellular_componentCul2-RING ubiquitin ligase complex
R0031463cellular_componentCul3-RING ubiquitin ligase complex
R0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
R0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
R0031466cellular_componentCul5-RING ubiquitin ligase complex
R0031467cellular_componentCul7-RING ubiquitin ligase complex
R0031625molecular_functionubiquitin protein ligase binding
R0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
R0032480biological_processnegative regulation of type I interferon production
R0034450molecular_functionubiquitin-ubiquitin ligase activity
R0034599biological_processcellular response to oxidative stress
R0034644biological_processcellular response to UV
R0042110biological_processT cell activation
R0042770biological_processsignal transduction in response to DNA damage
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
R0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
R0043687biological_processpost-translational protein modification
R0044314biological_processprotein K27-linked ubiquitination
R0044877molecular_functionprotein-containing complex binding
R0045116biological_processprotein neddylation
R0045732biological_processpositive regulation of protein catabolic process
R0046627biological_processnegative regulation of insulin receptor signaling pathway
R0046872molecular_functionmetal ion binding
R0060090molecular_functionmolecular adaptor activity
R0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
R0061630molecular_functionubiquitin protein ligase activity
R0061663molecular_functionNEDD8 ligase activity
R0062197biological_processcellular response to chemical stress
R0070936biological_processprotein K48-linked ubiquitination
R0071230biological_processcellular response to amino acid stimulus
R0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
R0090090biological_processnegative regulation of canonical Wnt signaling pathway
R0090734cellular_componentsite of DNA damage
R0097602molecular_functioncullin family protein binding
R0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
R0160240biological_processRNA polymerase II transcription initiation surveillance
R0160276biological_processnegative regulation of beige fat cell differentiation
R1900076biological_processregulation of cellular response to insulin stimulus
R1901525biological_processnegative regulation of mitophagy
R1902499biological_processpositive regulation of protein autoubiquitination
R1902883biological_processnegative regulation of response to oxidative stress
R1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN R 201
ChainResidue
RCYS42
RCYS45
RHIS80
RCYS83
site_idAC2
Number of Residues4
Detailsbinding site for residue ZN R 202
ChainResidue
RCYS53
RCYS56
RCYS68
RHIS82
site_idAC3
Number of Residues4
Detailsbinding site for residue ZN R 203
ChainResidue
RHIS77
RCYS94
RASP97
RCYS75
Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIevLIDKqYIeRsqasadeYsYvA
ChainResidueDetails
AILE718-ALA745
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"10092517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10597293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues9
DetailsRegion: {"description":"Interaction with Elongin BC complex"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues45
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues7
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_FI7
Number of Residues4
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_FI8
Number of Residues1
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_FI9
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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