3TGW
Crystal structure of subunit B mutant H156A of the 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 | 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 | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 461 |
| Chain | Residue |
| A | ILE185 |
| A | THR186 |
| A | ASN187 |
| A | LEU212 |
| A | ALA213 |
| A | ASP214 |
| A | HOH483 |
| A | HOH798 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE P33 A 5936 |
| Chain | Residue |
| A | ARG334 |
| A | LYS335 |
| A | GLY336 |
| A | HOH489 |
| A | HOH569 |
| A | HOH570 |
| A | HOH727 |
| A | HOH893 |
| A | HOH934 |
| B | THR21 |
| B | GLU22 |
| B | PRO23 |
| B | ALA49 |
| B | AES1474 |
| A | HIS333 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 462 |
| Chain | Residue |
| A | ASP125 |
| A | ARG142 |
| A | PRO170 |
| A | GLY171 |
| A | SER172 |
| A | GLY358 |
| A | HOH643 |
| A | HOH876 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 463 |
| Chain | Residue |
| A | MET34 |
| A | GLY35 |
| A | ASP36 |
| A | ARG40 |
| A | ASP109 |
| A | ALA113 |
| A | ALA114 |
| A | GOL465 |
| A | HOH1097 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 464 |
| Chain | Residue |
| A | LYS20 |
| A | THR21 |
| A | GLU22 |
| A | PRO23 |
| A | ALA49 |
| A | HOH981 |
| B | GLU204 |
| B | ARG205 |
| B | HOH648 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 465 |
| Chain | Residue |
| A | PRO14 |
| A | ARG40 |
| A | VAL56 |
| A | ALA113 |
| A | GOL463 |
| A | HOH1026 |
| B | ILE387 |
| B | VAL388 |
| B | HOH875 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 466 |
| Chain | Residue |
| A | TYR236 |
| A | HOH991 |
| A | HOH1036 |
| B | GLU237 |
| B | GOL463 |
| B | HOH898 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 467 |
| Chain | Residue |
| A | ASP316 |
| A | HOH486 |
| A | HOH601 |
| B | ARG334 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AES B 1474 |
| Chain | Residue |
| A | GLY336 |
| A | ARG413 |
| A | HOH626 |
| A | HOH754 |
| A | HOH898 |
| A | HOH909 |
| A | P335936 |
| B | LYS20 |
| B | PRO23 |
| B | VAL24 |
| B | TYR26 |
| B | ASP46 |
| B | SER47 |
| B | SER48 |
| B | HOH814 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 461 |
| Chain | Residue |
| B | ASP125 |
| B | ARG142 |
| B | HIS241 |
| B | ALA293 |
| B | HOH489 |
| B | HOH570 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 462 |
| Chain | Residue |
| A | ARG349 |
| B | THR137 |
| B | ASN138 |
| B | SER346 |
| B | SER368 |
| B | ASP369 |
| B | HOH480 |
| B | HOH538 |
| B | HOH566 |
| B | HOH1056 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG4 B 6112 |
| Chain | Residue |
| A | PHE149 |
| A | ILE321 |
| A | GLN325 |
| B | PHE149 |
| B | ILE321 |
| B | GLN325 |
| B | HOH779 |
| B | HOH780 |
| B | HOH932 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG0 B 6108 |
| Chain | Residue |
| A | MET115 |
| A | ASN116 |
| A | TYR236 |
| A | LYS291 |
| A | HOH817 |
| A | HOH1097 |
| B | ASN116 |
| B | TYR236 |
| B | LYS291 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 463 |
| Chain | Residue |
| A | GLN106 |
| A | GLU237 |
| A | GOL466 |
| A | HOH979 |
| A | HOH980 |
| B | TYR236 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 464 |
| Chain | Residue |
| B | TYR277 |
| B | ASP316 |
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 |
