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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1U6G

Crystal Structure of The Cand1-Cul1-Roc1 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000045biological_processautophagosome assembly
A0000082biological_processG1/S transition of mitotic cell cycle
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006915biological_processapoptotic process
A0007040biological_processlysosome organization
A0008283biological_processcell population proliferation
A0009887biological_processanimal organ morphogenesis
A0010507biological_processnegative regulation of autophagy
A0010508biological_processpositive regulation of autophagy
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0031669biological_processcellular response to nutrient levels
A0034599biological_processcellular response to oxidative stress
A0038202biological_processTORC1 signaling
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0070936biological_processprotein K48-linked ubiquitination
A0097193biological_processintrinsic apoptotic signaling pathway
A0140374biological_processantiviral innate immune response
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1904037biological_processpositive regulation of epithelial cell apoptotic process
A1904262biological_processnegative regulation of TORC1 signaling
A1990452cellular_componentParkin-FBXW7-Cul1 ubiquitin ligase complex
B0000045biological_processautophagosome assembly
B0000082biological_processG1/S transition of mitotic cell cycle
B0000165biological_processMAPK cascade
B0000209biological_processprotein polyubiquitination
B0000423biological_processmitophagy
B0001837biological_processepithelial to mesenchymal transition
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006283biological_processtranscription-coupled nucleotide-excision repair
B0006366biological_processtranscription by RNA polymerase II
B0006368biological_processtranscription elongation by RNA polymerase II
B0006511biological_processubiquitin-dependent protein catabolic process
B0006513biological_processprotein monoubiquitination
B0006915biological_processapoptotic process
B0006974biological_processDNA damage response
B0006979biological_processresponse to oxidative stress
B0007040biological_processlysosome organization
B0007283biological_processspermatogenesis
B0007346biological_processregulation of mitotic cell cycle
B0008270molecular_functionzinc ion binding
B0008286biological_processinsulin receptor signaling pathway
B0010507biological_processnegative regulation of autophagy
B0010508biological_processpositive regulation of autophagy
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0019005cellular_componentSCF ubiquitin ligase complex
B0019221biological_processcytokine-mediated signaling pathway
B0019788molecular_functionNEDD8 transferase activity
B0030163biological_processprotein catabolic process
B0030330biological_processDNA damage response, signal transduction by p53 class mediator
B0030891cellular_componentVCB complex
B0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
B0031461cellular_componentcullin-RING ubiquitin ligase complex
B0031462cellular_componentCul2-RING ubiquitin ligase complex
B0031463cellular_componentCul3-RING ubiquitin ligase complex
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
B0031466cellular_componentCul5-RING ubiquitin ligase complex
B0031467cellular_componentCul7-RING ubiquitin ligase complex
B0031625molecular_functionubiquitin protein ligase binding
B0031669biological_processcellular response to nutrient levels
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032480biological_processnegative regulation of type I interferon production
B0032481biological_processpositive regulation of type I interferon production
B0032869biological_processcellular response to insulin stimulus
B0034198biological_processcellular response to amino acid starvation
B0034450molecular_functionubiquitin-ubiquitin ligase activity
B0034599biological_processcellular response to oxidative stress
B0034644biological_processcellular response to UV
B0035279biological_processmiRNA-mediated gene silencing by mRNA destabilization
B0038066biological_processp38MAPK cascade
B0038202biological_processTORC1 signaling
B0042110biological_processT cell activation
B0042770biological_processsignal transduction in response to DNA damage
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0043687biological_processpost-translational protein modification
B0044877molecular_functionprotein-containing complex binding
B0045116biological_processprotein neddylation
B0045727biological_processpositive regulation of translation
B0045732biological_processpositive regulation of protein catabolic process
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046627biological_processnegative regulation of insulin receptor signaling pathway
B0046872molecular_functionmetal ion binding
B0060090molecular_functionmolecular adaptor activity
B0060337biological_processtype I interferon-mediated signaling pathway
B0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
B0061630molecular_functionubiquitin protein ligase activity
B0061663molecular_functionNEDD8 ligase activity
B0062197biological_processcellular response to chemical stress
B0070294biological_processrenal sodium ion absorption
B0070936biological_processprotein K48-linked ubiquitination
B0071230biological_processcellular response to amino acid stimulus
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0090090biological_processnegative regulation of canonical Wnt signaling pathway
B0090734cellular_componentsite of DNA damage
B0097510biological_processbase-excision repair, AP site formation via deaminated base removal
B0097602molecular_functioncullin family protein binding
B0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
B0160240biological_processRNA polymerase II transcription initiation surveillance
B1900076biological_processregulation of cellular response to insulin stimulus
B1901525biological_processnegative regulation of mitophagy
B1901797biological_processnegative regulation of signal transduction by p53 class mediator
B1902499biological_processpositive regulation of protein autoubiquitination
B1902883biological_processnegative regulation of response to oxidative stress
B1904037biological_processpositive regulation of epithelial cell apoptotic process
B1904262biological_processnegative regulation of TORC1 signaling
B1904263biological_processpositive regulation of TORC1 signaling
B2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
C0000151cellular_componentubiquitin ligase complex
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005794cellular_componentGolgi apparatus
C0005829cellular_componentcytosol
C0010265biological_processSCF complex assembly
C0016020cellular_componentmembrane
C0016567biological_processprotein ubiquitination
C0017025molecular_functionTBP-class protein binding
C0030154biological_processcell differentiation
C0031461cellular_componentcullin-RING ubiquitin ligase complex
C0034774cellular_componentsecretory granule lumen
C0043086biological_processnegative regulation of catalytic activity
C0045893biological_processpositive regulation of DNA-templated transcription
C0045899biological_processpositive regulation of RNA polymerase II transcription preinitiation complex assembly
C0070062cellular_componentextracellular exosome
C1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1229
ChainResidue
BCYS42
BCYS45
BHIS80
BCYS83
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1230
ChainResidue
BCYS75
BHIS77
BCYS94
BASP97
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1231
ChainResidue
BCYS56
BCYS68
BHIS82
BCYS53
Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIdiLIEKeYLeRvdgekdtYsYlA
ChainResidueDetails
AILE748-ALA775
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsDomain: {"description":"Cullin neddylation","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"10597293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15537541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18805092","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues45
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
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_FI5
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_FI6
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_FI7
Number of Residues37
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues34
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues34
DetailsRepeat: {"description":"HEAT 7"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues37
DetailsRepeat: {"description":"HEAT 9"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues43
DetailsRepeat: {"description":"HEAT 10"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues39
DetailsRepeat: {"description":"HEAT 11"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues37
DetailsRepeat: {"description":"HEAT 12"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues39
DetailsRepeat: {"description":"HEAT 13"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues37
DetailsRepeat: {"description":"HEAT 14"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues37
DetailsRepeat: {"description":"HEAT 15"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues37
DetailsRepeat: {"description":"HEAT 16"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues39
DetailsRepeat: {"description":"HEAT 17"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues36
DetailsRepeat: {"description":"HEAT 19"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues37
DetailsRepeat: {"description":"HEAT 20"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues37
DetailsRepeat: {"description":"HEAT 21"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues32
DetailsRepeat: {"description":"HEAT 22"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues37
DetailsRepeat: {"description":"HEAT 23"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues37
DetailsRepeat: {"description":"HEAT 24"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues54
DetailsRepeat: {"description":"HEAT 25"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues34
DetailsRepeat: {"description":"HEAT 26"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues49
DetailsRepeat: {"description":"HEAT 27"}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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