6UV2
Crystal structure of the core domain of RNA helicase DDX17 with RNA pri-125a-oligo1
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue ADP A 501 |
| Chain | Residue |
| A | PHE94 |
| A | THR143 |
| A | ASP404 |
| A | ARG432 |
| A | SER433 |
| A | BEF502 |
| A | MG503 |
| A | HOH655 |
| A | HOH675 |
| A | HOH697 |
| A | HOH726 |
| A | PHE112 |
| A | HOH741 |
| A | HOH743 |
| A | HOH790 |
| A | HOH800 |
| A | GLU114 |
| A | GLN119 |
| A | GLN137 |
| A | GLY139 |
| A | SER140 |
| A | GLY141 |
| A | LYS142 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue BEF A 502 |
| Chain | Residue |
| A | THR138 |
| A | GLY139 |
| A | LYS142 |
| A | GLU247 |
| A | GLY402 |
| A | ARG429 |
| A | ARG432 |
| A | ADP501 |
| A | MG503 |
| A | HOH726 |
| A | HOH735 |
| A | HOH736 |
| A | HOH787 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | ADP501 |
| A | BEF502 |
| A | HOH697 |
| A | HOH726 |
| A | HOH735 |
| A | HOH736 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 504 |
| Chain | Residue |
| A | ARG130 |
| A | ASP131 |
| A | ARG293 |
| A | ASP294 |
| A | MG505 |
| A | HOH786 |
| A | HOH892 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 505 |
| Chain | Residue |
| A | LYS53 |
| A | GLY129 |
| A | ASP131 |
| A | GLN272 |
| A | MG504 |
| A | HOH786 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 506 |
| Chain | Residue |
| A | ASN302 |
| A | GLU304 |
| A | SER306 |
| A | HOH775 |
| A | HOH776 |
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 | VAL244-LEU252 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 175 |
| 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 | 147 |
| 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 | 28 |
| Details | Motif: {"description":"Q motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEAD box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| 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 |
