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 | 6 |
Details | BINDING SITE FOR RESIDUE MPD A 589 |
Chain | Residue |
A | HIS245 |
A | GLN246 |
A | LYS249 |
A | ILE475 |
A | VAL479 |
A | ALA507 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MPD A 590 |
Chain | Residue |
A | LEU364 |
A | TYR368 |
A | GLY390 |
A | ALA391 |
A | ALA330 |
A | ASP331 |
A | SER332 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MPD A 591 |
Chain | Residue |
A | GLU454 |
A | MET458 |
A | LYS461 |
A | LEU528 |
A | ASP532 |
A | HOH759 |
A | HOH834 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 592 |
Chain | Residue |
A | LYS461 |
A | ALA464 |
A | TYR531 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY A 593 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MPD A 594 |
Chain | Residue |
A | GLU581 |
A | LYS585 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY A 595 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY A 596 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY A 597 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 598 |
Chain | Residue |
A | ASP270 |
A | PHE275 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TRS A 599 |
Chain | Residue |
A | LYS198 |
A | TYR201 |
A | LYS202 |
A | HOH747 |
A | HOH836 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS A 600 |
Chain | Residue |
A | ASP420 |
A | LEU421 |
A | ARG424 |
A | ASN431 |
A | TRP432 |
A | LEU433 |
A | HOH624 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TRS A 601 |
Chain | Residue |
A | LYS123 |
A | ALA124 |
A | ASP128 |
A | ASP134 |
A | ILE135 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 602 |
Chain | Residue |
A | ARG489 |
A | LEU492 |
A | ARG496 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 603 |
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 | |