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 | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 589 |
Chain | Residue |
A | LYS198 |
A | PRO200 |
A | TYR201 |
A | LYS202 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 590 |
Chain | Residue |
A | ALA464 |
A | LEU465 |
A | LYS468 |
A | TYR531 |
A | HOH879 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD A 591 |
Chain | Residue |
A | ASP420 |
A | ASN431 |
A | TRP432 |
A | LEU433 |
A | HOH683 |
A | HOH743 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TRS A 592 |
Chain | Residue |
A | GLU454 |
A | MET458 |
A | LYS461 |
A | ASN529 |
A | ASP532 |
A | HOH713 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 593 |
Chain | Residue |
A | LYS198 |
A | HOH1007 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 594 |
Chain | Residue |
A | GLU161 |
A | VAL173 |
A | ILE174 |
A | ALA175 |
A | HOH783 |
A | HOH898 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 595 |
Chain | Residue |
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 | |