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 | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 589 |
| Chain | Residue |
| A | HIS245 |
| A | GLN246 |
| A | LYS249 |
| A | ILE475 |
| A | ALA507 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 590 |
| Chain | Residue |
| A | HOH687 |
| A | HOH846 |
| A | HOH847 |
| A | GLU454 |
| A | MET458 |
| A | LYS461 |
| A | ASP532 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS A 591 |
| Chain | Residue |
| A | ILE184 |
| A | PRO551 |
| A | GLU581 |
| A | HOH702 |
| A | HOH774 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 592 |
| Chain | Residue |
| A | ALA330 |
| A | SER332 |
| A | THR333 |
| A | PHE367 |
| A | TYR368 |
| A | ALA391 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 593 |
| Chain | Residue |
| A | LEU421 |
| A | ASN431 |
| A | LEU433 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 594 |
| Chain | Residue |
| A | LYS198 |
| A | PRO200 |
| A | TYR201 |
| A | HOH604 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY A 595 |
| Chain | Residue |
| A | VAL173 |
| A | HOH837 |
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 | |
