Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
A | 0033178 | cellular_component | proton-transporting two-sector ATPase complex, catalytic domain |
A | 0046034 | biological_process | ATP metabolic process |
A | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | binding site for residue ACY A 601 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue TRS A 603 |
Chain | Residue |
A | GLU183 |
A | ILE184 |
A | GLU581 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MPD A 604 |
Chain | Residue |
A | ILE475 |
A | ALA507 |
A | VAL242 |
A | HIS245 |
A | GLN246 |
A | LYS249 |
A | LEU278 |
Functional Information from PROSITE/UniProt
site_id | PS00152 |
Number of Residues | 10 |
Details | ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINWLTSYS |
Chain | Residue | Details |
A | PRO428-SER437 | |