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8TL6

Cryo-EM structure of DDB1deltaB-DDA1-DCAF5

Functional Information from GO Data
ChainGOidnamespacecontents
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0016567biological_processprotein ubiquitination
B0045717biological_processnegative regulation of fatty acid biosynthetic process
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
E0000209biological_processprotein polyubiquitination
E0005515molecular_functionprotein binding
E0005654cellular_componentnucleoplasm
E0016567biological_processprotein ubiquitination
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-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
EALA2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ESER33
BSER533
BSER626
BSER628

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ESER95
BSER794

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER648

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BSER651

219869

PDB entries from 2024-05-15

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