Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003724 | molecular_function | RNA helicase activity |
| A | 0005524 | molecular_function | ATP binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003724 | molecular_function | RNA helicase activity |
| B | 0005524 | molecular_function | ATP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1 |
| Chain | Residue |
| A | THR225 |
| A | GLY226 |
| A | SER227 |
| A | GLY228 |
| A | LYS229 |
| A | THR230 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 388 |
| Chain | Residue |
| A | GLY342 |
| A | GLU346 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 389 |
| Chain | Residue |
| A | LYS229 |
| A | GLU334 |
| A | SER364 |
| A | ALA365 |
| A | ALA223 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SCN A 390 |
| Chain | Residue |
| A | THR308 |
| A | GLY310 |
| A | ARG311 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SCN B 2 |
| Chain | Residue |
| B | THR308 |
| B | GLY310 |
| B | ARG311 |
Functional Information from PROSITE/UniProt
| site_id | PS00039 |
| Number of Residues | 9 |
| Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VIDEADRiL |
| Chain | Residue | Details |
| A | VAL331-LEU339 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 350 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DEAD box"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
