6TD3
Structure of DDB1 bound to CR8-engaged CDK12-cyclinK
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0005634 | cellular_component | nucleus |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| C | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0005634 | cellular_component | nucleus |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| F | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| F | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
| G | 0003676 | molecular_function | nucleic acid binding |
| G | 0005634 | cellular_component | nucleus |
| H | 0004672 | molecular_function | protein kinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006468 | biological_process | protein phosphorylation |
| I | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| I | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue RC8 B 1101 |
| Chain | Residue |
| A | ASN907 |
| B | ASP817 |
| B | HIS818 |
| B | ASP819 |
| B | LEU866 |
| A | ARG928 |
| A | ARG947 |
| B | ILE733 |
| B | ALA754 |
| B | PHE813 |
| B | GLU814 |
| B | TYR815 |
| B | MET816 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue RC8 E 1101 |
| Chain | Residue |
| D | ASN907 |
| D | ARG928 |
| D | ARG947 |
| E | ILE733 |
| E | ALA754 |
| E | PHE813 |
| E | GLU814 |
| E | TYR815 |
| E | MET816 |
| E | ASP817 |
| E | HIS818 |
| E | ASP819 |
| E | LEU866 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue RC8 H 1101 |
| Chain | Residue |
| G | ASN907 |
| G | ARG928 |
| G | ARG947 |
| H | ILE733 |
| H | ALA754 |
| H | PHE813 |
| H | GLU814 |
| H | TYR815 |
| H | MET816 |
| H | ASP817 |
| H | HIS818 |
| H | ASP819 |
| H | LEU866 |
| H | ASP877 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGQVYkAkdkdtgel..........VALK |
| Chain | Residue | Details |
| B | ILE733-LYS756 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FlHrDIKcsNILL |
| Chain | Residue | Details |
| B | PHE855-LEU867 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1029 |
| Details | Region: {"description":"WD repeat beta-propeller A"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1002 |
| Details | Region: {"description":"WD repeat beta-propeller C"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1107 |
| Details | Region: {"description":"Interaction with CDT1 and CUL4A","evidences":[{"source":"PubMed","id":"15448697","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 45 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24662513","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
