3SSA
Crystal structure of subunit B mutant N157T of the 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 | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 461 |
| Chain | Residue |
| A | PRO23 |
| A | HOH507 |
| A | HOH549 |
| B | HIS238 |
| B | HOH495 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 462 |
| Chain | Residue |
| A | ASP316 |
| A | HOH489 |
| A | HOH756 |
| B | ARG334 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 463 |
| Chain | Residue |
| A | ASP97 |
| A | GLY99 |
| A | LYS447 |
| A | HOH1016 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 464 |
| Chain | Residue |
| A | HIS333 |
| A | HOH702 |
| A | AES1474 |
| A | PEG6073 |
| B | LYS20 |
| B | THR21 |
| B | PRO23 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AES A 1474 |
| Chain | Residue |
| A | GLY336 |
| A | ASP409 |
| A | ARG413 |
| A | 1PE464 |
| A | HOH681 |
| A | HOH713 |
| A | HOH762 |
| A | HOH898 |
| B | LYS20 |
| B | PRO23 |
| B | VAL24 |
| B | TYR26 |
| B | SER47 |
| B | SER48 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 465 |
| Chain | Residue |
| A | HIS156 |
| A | THR157 |
| A | GLU189 |
| A | THR247 |
| A | ASP248 |
| A | HOH889 |
| A | HOH1073 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE A 466 |
| Chain | Residue |
| A | PHE149 |
| A | ILE321 |
| A | GLN325 |
| A | HOH938 |
| B | PHE149 |
| B | GLN325 |
| B | VAL327 |
| B | HOH555 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 467 |
| Chain | Residue |
| A | LEU393 |
| A | SER394 |
| A | ASP397 |
| B | ASN116 |
| B | HOH658 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 468 |
| Chain | Residue |
| A | ILE70 |
| A | HOH1065 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 469 |
| Chain | Residue |
| A | ILE185 |
| A | THR186 |
| A | ASN187 |
| A | LEU212 |
| A | ALA213 |
| A | ASP214 |
| A | HOH916 |
| A | HOH968 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 6073 |
| Chain | Residue |
| A | TYR192 |
| A | 1PE464 |
| A | HOH693 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 470 |
| Chain | Residue |
| A | GLU427 |
| A | LYS451 |
| A | TYR452 |
| A | HIS453 |
| A | PRO454 |
| A | HIS456 |
| A | HOH590 |
| A | HOH977 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PGE A 471 |
| Chain | Residue |
| A | ALA113 |
| A | MET115 |
| A | ASN116 |
| A | TYR236 |
| A | LYS291 |
| A | HOH809 |
| B | ASN116 |
| B | TYR236 |
| B | LYS291 |
| B | GOL462 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 461 |
| Chain | Residue |
| B | LYS124 |
| B | ASP125 |
| B | ARG142 |
| B | HIS241 |
| B | ALA293 |
| B | HOH820 |
| B | PEG6073 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 462 |
| Chain | Residue |
| A | GLN106 |
| A | GLU237 |
| A | PGE471 |
| B | TYR236 |
| B | PEG465 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 463 |
| Chain | Residue |
| A | GLU22 |
| A | PRO23 |
| A | ALA49 |
| A | HOH951 |
| B | GLU204 |
| A | LYS20 |
| A | THR21 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 464 |
| Chain | Residue |
| B | SER90 |
| B | SER92 |
| B | GLU219 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG B 6073 |
| Chain | Residue |
| B | ARG142 |
| B | PRO170 |
| B | GLY171 |
| B | SER172 |
| B | HIS241 |
| B | GOL461 |
| B | HOH594 |
| B | HOH746 |
| B | HOH1013 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 465 |
| Chain | Residue |
| A | TYR236 |
| A | HOH912 |
| B | GLN106 |
| B | GLU237 |
| B | GOL462 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 466 |
| Chain | Residue |
| A | HOH1027 |
| B | THR137 |
| B | SER368 |
| B | ASP369 |
| B | TYR372 |
| B | HOH552 |
| B | HOH930 |
| B | HOH1044 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 467 |
| Chain | Residue |
| A | HOH982 |
| B | LEU384 |
| B | ALA392 |
| B | LEU393 |
| B | SER394 |
| B | ASP397 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 468 |
| Chain | Residue |
| B | TYR277 |
| B | ASP316 |
| B | HOH545 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 469 |
| Chain | Residue |
| B | GLU158 |
| B | ARG416 |
| B | HOH634 |
| B | HOH824 |
| B | HOH1000 |
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 |
