8SZP
Human DHX9 bound to ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003725 | molecular_function | double-stranded RNA binding |
A | 0005524 | molecular_function | ATP binding |
A | 0033679 | molecular_function | 3'-5' DNA/RNA helicase activity |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003725 | molecular_function | double-stranded RNA binding |
B | 0005524 | molecular_function | ATP binding |
B | 0033679 | molecular_function | 3'-5' DNA/RNA helicase activity |
Functional Information from PROSITE/UniProt
site_id | PS00690 |
Number of Residues | 10 |
Details | DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. ShVIVDEIHE |
Chain | Residue | Details |
A | SER506-GLU515 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11416126, ECO:0000269|PubMed:20510246, ECO:0007744|PDB:3LLM |
Chain | Residue | Details |
A | GLY411 | |
B | GLY411 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20510246, ECO:0007744|PDB:3LLM |
Chain | Residue | Details |
A | THR418 | |
A | GLU512 | |
B | THR418 | |
B | GLU512 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS191 | |
A | LYS199 | |
A | LYS1024 | |
B | LYS191 | |
B | LYS199 | |
B | LYS1024 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER321 | |
B | SER321 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER449 | |
A | SER506 | |
B | SER449 | |
B | SER506 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS697 | |
B | LYS697 |