7ZMM
Crystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G2-001
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006310 | biological_process | DNA recombination |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004386 | molecular_function | helicase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006310 | biological_process | DNA recombination |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004386 | molecular_function | helicase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006310 | biological_process | DNA recombination |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004386 | molecular_function | helicase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006310 | biological_process | DNA recombination |
Functional Information from PROSITE/UniProt
| site_id | PS00690 |
| Number of Residues | 10 |
| Details | DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC |
| Chain | Residue | Details |
| B | SER152-CYS161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA |
| Chain | Residue | Details |
| B | GLY55 | |
| B | ALA56 | |
| B | GLY57 | |
| B | LYS58 | |
| B | SER59 | |
| A | PHE26 | |
| A | SER28 | |
| A | LYS30 | |
| A | GLN34 | |
| A | GLY55 | |
| A | ALA56 | |
| A | GLY57 | |
| A | LYS58 | |
| A | SER59 | |
| C | PHE26 | |
| C | SER28 | |
| C | LYS30 | |
| C | GLN34 | |
| C | GLY55 | |
| C | ALA56 | |
| C | GLY57 | |
| C | LYS58 | |
| C | SER59 | |
| D | PHE26 | |
| D | SER28 | |
| D | LYS30 | |
| D | GLN34 | |
| D | GLY55 | |
| D | ALA56 | |
| D | GLY57 | |
| D | LYS58 | |
| D | SER59 | |
| B | PHE26 | |
| B | SER28 | |
| B | LYS30 | |
| B | GLN34 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:5LB5 |
| Chain | Residue | Details |
| B | PRO53 | |
| A | PRO53 | |
| C | PRO53 | |
| D | PRO53 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8, ECO:0007744|PDB:5LBA |
| Chain | Residue | Details |
| B | CYS411 | |
| B | CYS431 | |
| B | CYS434 | |
| A | CYS411 | |
| A | CYS431 | |
| A | CYS434 | |
| C | CYS411 | |
| C | CYS431 | |
| C | CYS434 | |
| D | CYS411 | |
| D | CYS431 | |
| D | CYS434 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA |
| Chain | Residue | Details |
| B | CYS427 | |
| A | CYS427 | |
| C | CYS427 | |
| D | CYS427 |
