1F2U
Crystal Structure of RAD50 ABC-ATPase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006302 | biological_process | double-strand break repair |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0006302 | biological_process | double-strand break repair |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 902 |
| Chain | Residue |
| A | SER37 |
| A | GLN140 |
| A | ATP901 |
| A | HOH914 |
| B | HOH48 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 902 |
| Chain | Residue |
| D | HOH50 |
| C | SER37 |
| C | GLN140 |
| C | ATP901 |
| C | HOH919 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ATP A 901 |
| Chain | Residue |
| A | ARG12 |
| A | GLN31 |
| A | ASN32 |
| A | GLY33 |
| A | SER34 |
| A | GLY35 |
| A | LYS36 |
| A | SER37 |
| A | SER38 |
| A | GLU60 |
| A | THR62 |
| A | LYS63 |
| A | VAL64 |
| A | GLN140 |
| A | MG902 |
| A | HOH907 |
| A | HOH908 |
| A | HOH914 |
| A | HOH947 |
| B | HOH48 |
| B | HOH260 |
| B | GLU823 |
| D | HOH162 |
| D | LYS763 |
| D | TYR764 |
| D | PHE791 |
| D | SER793 |
| D | GLY794 |
| D | GLY795 |
| D | GLU796 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE ATP C 901 |
| Chain | Residue |
| B | HOH12 |
| B | HOH283 |
| B | LYS763 |
| B | TYR764 |
| B | PHE791 |
| B | SER793 |
| B | GLY794 |
| B | GLY795 |
| B | GLU796 |
| C | ARG12 |
| C | SER13 |
| C | GLN31 |
| C | ASN32 |
| C | GLY33 |
| C | SER34 |
| C | GLY35 |
| C | LYS36 |
| C | SER37 |
| C | SER38 |
| C | GLU60 |
| C | THR62 |
| C | LYS63 |
| C | VAL64 |
| C | GLN140 |
| C | MG902 |
| C | HOH903 |
| C | HOH908 |
| C | HOH919 |
| C | HOH929 |
| C | HOH933 |
| D | HOH50 |
| D | GLU823 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT |
| Chain | Residue | Details |
| B | LYS763 | |
| B | PHE791 | |
| D | LYS763 | |
| D | PHE791 | |
| C | ASN32 | |
| C | GLU60 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU |
| Chain | Residue | Details |
| A | GLN140 | |
| C | GLN140 |
