7LIU
DDX3X bound to ATP analog and remodeled RNA:DNA hybrid
Functional Information from GO Data
Functional Information from PROSITE/UniProt
| site_id | PS00039 |
| Number of Residues | 9 |
| Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADRmL |
| Chain | Residue | Details |
| A | VAL345-LEU353 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 384 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 322 |
| Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 66 |
| Details | Region: {"description":"Interaction with CHUK","evidences":[{"source":"PubMed","id":"17667941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Region: {"description":"Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 56 |
| Details | Motif: {"description":"Q motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DEAD box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine; by TBK1; in vitro","evidences":[{"source":"PubMed","id":"18583960","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by TBK1","evidences":[{"source":"PubMed","id":"18583960","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by CSNK1E and TBK1; in vitro","evidences":[{"source":"PubMed","id":"18583960","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29222110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by TBK1; in vitro","evidences":[{"source":"PubMed","id":"18583960","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by CSNK1E; in vitro","evidences":[{"source":"PubMed","id":"29222110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by CSNK1E; in vitro","evidences":[{"source":"PubMed","id":"29222110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
