Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6SJ7

Structure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to RBM39 and Indisulam

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0002376biological_processimmune system process
A0005515molecular_functionprotein binding
A0016567biological_processprotein ubiquitination
A0032814biological_processregulation of natural killer cell activation
A0036094molecular_functionsmall molecule binding
A0046872molecular_functionmetal ion binding
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0000781cellular_componentchromosome, telomeric region
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006974biological_processDNA damage response
B0007056biological_processspindle assembly involved in female meiosis
B0007283biological_processspermatogenesis
B0008283biological_processcell population proliferation
B0010498biological_processproteasomal protein catabolic process
B0010506biological_processregulation of autophagy
B0016567biological_processprotein ubiquitination
B0019076biological_processviral release from host cell
B0030174biological_processregulation of DNA-templated DNA replication initiation
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031297biological_processreplication fork processing
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
B0032814biological_processregulation of natural killer cell activation
B0032991cellular_componentprotein-containing complex
B0034644biological_processcellular response to UV
B0035861cellular_componentsite of double-strand break
B0040029biological_processepigenetic regulation of gene expression
B0042127biological_processregulation of cell population proliferation
B0042752biological_processregulation of circadian rhythm
B0042981biological_processregulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044725biological_processepigenetic programming in the zygotic pronuclei
B0044877molecular_functionprotein-containing complex binding
B0045070biological_processpositive regulation of viral genome replication
B0045722biological_processpositive regulation of gluconeogenesis
B0045732biological_processpositive regulation of protein catabolic process
B0045995biological_processregulation of embryonic development
B0046726biological_processpositive regulation by virus of viral protein levels in host cell
B0048511biological_processrhythmic process
B0051702biological_processbiological process involved in interaction with symbiont
B0060964biological_processregulation of miRNA-mediated gene silencing
B0070062cellular_componentextracellular exosome
B0070914biological_processUV-damage excision repair
B0071987molecular_functionWD40-repeat domain binding
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0080135biological_processregulation of cellular response to stress
B0097602molecular_functioncullin family protein binding
B0160072molecular_functionubiquitin ligase complex scaffold activity
B1901987biological_processregulation of cell cycle phase transition
B1901990biological_processregulation of mitotic cell cycle phase transition
B1902412biological_processregulation of mitotic cytokinesis
B1904178biological_processnegative regulation of adipose tissue development
B2000036biological_processregulation of stem cell population maintenance
C0003676molecular_functionnucleic acid binding
C0003723molecular_functionRNA binding
C0005634cellular_componentnucleus
C0006397biological_processmRNA processing
D0000209biological_processprotein polyubiquitination
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0016567biological_processprotein ubiquitination
D0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0032814biological_processregulation of natural killer cell activation
D0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue EF6 A 701
ChainResidue
ATHR230
APHE231
AGLN232
APRO233
AALA234
APHE235
CASN260
CASP264
CMET265
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31686031","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31693911","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PAI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31686031","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31693911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31819272","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PAI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31686031","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31693911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31819272","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PAI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q0W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

PDB statisticsPDBj update infoContact PDBjnumon