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 |
| A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 589 |
| Chain | Residue |
| A | HIS245 |
| A | GLN246 |
| A | LYS249 |
| A | LYS279 |
| A | VAL479 |
| A | ALA507 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY A 590 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY A 591 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY A 592 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 594 |
| Chain | Residue |
| A | ALA457 |
| A | LYS461 |
| A | HOH685 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS A 595 |
| Chain | Residue |
| A | ILE451 |
| A | ASP452 |
| A | VAL521 |
| A | ARG525 |
| A | HOH777 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY A 596 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY A 598 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 599 |
| Chain | Residue |
| A | GLU555 |
| A | GLU562 |
| A | LYS567 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 600 |
| Chain | Residue |
| A | PRO551 |
| A | GLU581 |
| A | LYS585 |
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 | |