Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8G46

Cryo-EM structure of DDB1deltaB-DDA1-DCAF16-BRD4(BD2)-MMH2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005634cellular_componentnucleus
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0016567biological_processprotein ubiquitination
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
E0000209biological_processprotein polyubiquitination
E0005515molecular_functionprotein binding
E0005654cellular_componentnucleoplasm
E0016567biological_processprotein ubiquitination
E0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
E0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
E0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330
ChainResidueDetails
ASER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1067

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9ESW0
ChainResidueDetails
ATHR1125

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS1121

220113

PDB entries from 2024-05-22

PDB statisticsPDBj update infoContact PDBjnumon