8ROX
Structure of the human DDB1-DDA1-DCAF15 E3 ubiquitin ligase bound to compound furan 12
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000209 | biological_process | protein polyubiquitination |
| A | 0002376 | biological_process | immune system process |
| A | 0005515 | molecular_function | protein binding |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0032814 | biological_process | regulation of natural killer cell activation |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0080008 | cellular_component | Cul4-RING E3 ubiquitin ligase complex |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0005634 | cellular_component | nucleus |
| D | 0000209 | biological_process | protein polyubiquitination |
| D | 0005515 | molecular_function | protein binding |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0016567 | biological_process | protein ubiquitination |
| D | 0032434 | biological_process | regulation of proteasomal ubiquitin-dependent protein catabolic process |
| D | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| D | 0032814 | biological_process | regulation of natural killer cell activation |
| D | 0080008 | cellular_component | Cul4-RING E3 ubiquitin ligase complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified 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"}]} |
| Chain | Residue | Details |
