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 | 0016887 | molecular_function | ATP hydrolysis activity |
| 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 |
| A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 589 |
| Chain | Residue |
| 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 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | LEU438 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | ARG264 | |
| A | GLU263 | |
| A | LYS240 | |
