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 | 0006754 | biological_process | ATP biosynthetic process |
A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
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 | 0006754 | biological_process | ATP biosynthetic process |
B | 0015986 | biological_process | proton motive force-driven ATP synthesis |
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 |