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 | 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 | 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 |