3QKT
Rad50 ABC-ATPase with adjacent coiled-coil region in complex with AMP-PNP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006302 | biological_process | double-strand break repair |
A | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006302 | biological_process | double-strand break repair |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006302 | biological_process | double-strand break repair |
C | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006302 | biological_process | double-strand break repair |
D | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE ANP A 901 |
Chain | Residue |
A | ARG12 |
A | SER38 |
A | GLU60 |
A | THR62 |
A | LYS63 |
A | VAL64 |
A | GLN140 |
A | HOH314 |
A | HOH685 |
A | GLU823 |
A | HOH883 |
A | SER13 |
A | HOH890 |
A | HOH891 |
A | MG902 |
A | HOH905 |
B | LYS763 |
B | TYR764 |
B | PHE791 |
B | SER793 |
B | GLY794 |
B | GLY795 |
A | GLN31 |
B | GLU796 |
B | HOH892 |
A | ASN32 |
A | GLY33 |
A | SER34 |
A | GLY35 |
A | LYS36 |
A | SER37 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 902 |
Chain | Residue |
A | SER37 |
A | GLN140 |
A | HOH685 |
A | HOH883 |
A | ANP901 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE ANP B 901 |
Chain | Residue |
A | LYS763 |
A | TYR764 |
A | PHE791 |
A | SER793 |
A | GLY794 |
A | GLY795 |
A | GLU796 |
A | HOH885 |
B | ARG12 |
B | SER13 |
B | GLN31 |
B | ASN32 |
B | GLY33 |
B | SER34 |
B | GLY35 |
B | LYS36 |
B | SER37 |
B | SER38 |
B | GLU60 |
B | THR62 |
B | LYS63 |
B | VAL64 |
B | GLN140 |
B | GLU823 |
B | HOH883 |
B | HOH889 |
B | HOH893 |
B | MG902 |
B | HOH918 |
B | HOH920 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 902 |
Chain | Residue |
B | SER37 |
B | GLN140 |
B | HOH684 |
B | HOH883 |
B | ANP901 |
site_id | AC5 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE ANP C 901 |
Chain | Residue |
D | GLY795 |
D | 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 | HOH184 |
C | HOH701 |
C | GLU823 |
C | HOH886 |
C | HOH894 |
C | MG902 |
C | HOH922 |
C | HOH924 |
D | LYS763 |
D | TYR764 |
D | PHE791 |
D | SER793 |
D | GLY794 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 902 |
Chain | Residue |
C | SER37 |
C | GLN140 |
C | HOH603 |
C | HOH701 |
C | ANP901 |
site_id | AC7 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE ANP D 901 |
Chain | Residue |
C | LYS763 |
C | TYR764 |
C | PHE791 |
C | SER793 |
C | GLY794 |
C | GLY795 |
C | GLU796 |
C | HOH891 |
D | ARG12 |
D | SER13 |
D | GLN31 |
D | ASN32 |
D | GLY33 |
D | SER34 |
D | GLY35 |
D | LYS36 |
D | SER37 |
D | SER38 |
D | GLU60 |
D | THR62 |
D | LYS63 |
D | VAL64 |
D | GLN140 |
D | HOH189 |
D | GLU823 |
D | HOH884 |
D | MG902 |
D | HOH905 |
D | HOH908 |
D | HOH921 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 902 |
Chain | Residue |
D | SER37 |
D | GLN140 |
D | HOH702 |
D | HOH884 |
D | ANP901 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0000269|PubMed:24493214, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT, ECO:0007744|PDB:3QKU, ECO:0007744|PDB:4NCJ |
Chain | Residue | Details |
A | ARG12 | |
D | ARG12 | |
D | ASN32 | |
D | GLU60 | |
A | ASN32 | |
A | GLU60 | |
B | ARG12 | |
B | ASN32 | |
B | GLU60 | |
C | ARG12 | |
C | ASN32 | |
C | GLU60 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
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 | |
B | GLN140 | |
C | GLN140 | |
D | GLN140 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10892749, ECO:0000269|PubMed:21441914, ECO:0007744|PDB:1F2U, ECO:0007744|PDB:3QKT |
Chain | Residue | Details |
A | LYS763 | |
A | PHE791 | |
B | LYS763 | |
B | PHE791 | |
C | LYS763 | |
C | PHE791 | |
D | LYS763 | |
D | PHE791 |