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 |