6O5F
Crystal structure of DEAD-box RNA helicase DDX3X at pre-unwound state
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 701 |
| Chain | Residue |
| A | THR323 |
| A | GLY325 |
| A | ARG326 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 702 |
| Chain | Residue |
| A | SER476 |
| A | GLN477 |
| A | ARG478 |
| B | ASN173 |
| B | HOH821 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CL A 703 |
| Chain | Residue |
| A | PRO267 |
| A | GLY337 |
| A | LEU338 |
| A | ASP339 |
| A | PHE340 |
| A | CYS341 |
| A | TYR266 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 704 |
| Chain | Residue |
| A | GLY227 |
| A | SER228 |
| A | GLY229 |
| A | LYS230 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 701 |
| Chain | Residue |
| B | THR323 |
| B | GLY325 |
| B | ARG326 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 702 |
| Chain | Residue |
| B | TYR266 |
| B | PRO267 |
| B | GLY337 |
| B | LEU338 |
| B | ASP339 |
| B | PHE340 |
| B | CYS341 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 703 |
| Chain | Residue |
| A | GLY172 |
| A | ASN173 |
| B | SER476 |
| B | GLN477 |
| B | ARG478 |
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 | 56 |
| Details | Motif: {"description":"Q motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DEAD box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| 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_FI6 |
| 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_FI7 |
| 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_FI8 |
| 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_FI9 |
| 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_FI10 |
| 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 |
