3B2Q
Intermediate position of ATP on its trail to the binding pocket inside the subunit B mutant R416W of the energy converter A1Ao ATP synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006754 | biological_process | ATP biosynthetic process |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
| A | 0016020 | cellular_component | membrane |
| A | 0033178 | cellular_component | proton-transporting two-sector ATPase complex, catalytic domain |
| A | 0042777 | biological_process | proton motive force-driven plasma membrane ATP synthesis |
| A | 0046034 | biological_process | ATP metabolic process |
| A | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006754 | biological_process | ATP biosynthetic process |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0015986 | biological_process | proton motive force-driven ATP synthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0033178 | cellular_component | proton-transporting two-sector ATPase complex, catalytic domain |
| B | 0042777 | biological_process | proton motive force-driven plasma membrane ATP synthesis |
| B | 0046034 | biological_process | ATP metabolic process |
| B | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
| B | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP A 461 |
| Chain | Residue |
| A | PHE149 |
| A | PRO345 |
| B | PHE149 |
| B | ILE314 |
| B | PRO315 |
| B | ASP316 |
| B | SER318 |
| B | GLN325 |
| B | HOH889 |
| A | ALA151 |
| A | SER318 |
| A | ILE321 |
| A | GLN325 |
| A | VAL327 |
| A | VAL328 |
| A | ALA329 |
| A | ARG330 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AES B 462 |
| Chain | Residue |
| A | ARG413 |
| A | HOH463 |
| A | HOH557 |
| B | LYS20 |
| B | PRO23 |
| B | VAL24 |
| B | TYR26 |
| B | ASP46 |
| B | SER47 |
| B | CIT463 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CIT B 463 |
| Chain | Residue |
| A | HIS333 |
| A | GLY336 |
| A | HOH520 |
| B | LYS20 |
| B | AES462 |
| B | HOH1079 |
| B | HOH1137 |
Functional Information from PROSITE/UniProt
| site_id | PS00152 |
| Number of Residues | 10 |
| Details | ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PPINVLPSLS |
| Chain | Residue | Details |
| A | PRO339-SER348 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| A | ARG349 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ohh |
| Chain | Residue | Details |
| B | ARG349 |
