3TIV
Crystal structure of subunit B mutant N157A 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 | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 461 |
Chain | Residue |
A | THR137 |
A | HOH809 |
B | ARG349 |
A | ASN138 |
A | SER346 |
A | MET351 |
A | SER368 |
A | ASP369 |
A | TYR372 |
A | HOH806 |
A | HOH807 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 462 |
Chain | Residue |
A | LYS124 |
A | ASP125 |
A | ARG142 |
A | HIS241 |
A | ALA293 |
A | HOH818 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 463 |
Chain | Residue |
A | ARG87 |
A | ASP97 |
A | LYS447 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 464 |
Chain | Residue |
A | PHE149 |
A | SER150 |
A | MET305 |
A | VAL328 |
A | ALA329 |
A | ARG330 |
B | ASP316 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 465 |
Chain | Residue |
A | ILE185 |
A | THR186 |
A | ASN187 |
A | GLU188 |
A | LEU212 |
A | ALA213 |
A | ASP214 |
A | HOH1105 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 466 |
Chain | Residue |
B | LEU384 |
B | ALA392 |
B | LEU393 |
B | SER394 |
B | ASP397 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG0 A 6108 |
Chain | Residue |
A | GLY35 |
A | MET115 |
A | HOH492 |
A | HOH591 |
B | TYR236 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 467 |
Chain | Residue |
A | MET115 |
A | ASN116 |
A | TYR236 |
A | LYS291 |
A | HOH678 |
B | MET115 |
B | ASN116 |
B | TYR236 |
B | LYS291 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 468 |
Chain | Residue |
A | LYS20 |
A | GLU22 |
A | PRO23 |
A | ALA49 |
B | GLU204 |
B | ARG205 |
B | HOH553 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GOL B 461 |
Chain | Residue |
A | ARG349 |
B | THR137 |
B | ASN138 |
B | SER346 |
B | SER368 |
B | ASP369 |
B | TYR372 |
B | HOH472 |
B | HOH473 |
B | HOH728 |
B | HOH814 |
B | HOH873 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 462 |
Chain | Residue |
B | LYS124 |
B | ASP125 |
B | ARG142 |
B | HIS241 |
B | ALA293 |
B | HOH715 |
B | HOH798 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PG4 B 6112 |
Chain | Residue |
A | PHE149 |
A | SER318 |
A | ILE321 |
A | GLN325 |
B | PHE149 |
B | GLN325 |
B | HOH525 |
B | HOH526 |
B | HOH938 |
site_id | BC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AES B 1474 |
Chain | Residue |
B | SER48 |
B | 1PE463 |
A | GLY336 |
A | ASP409 |
A | ARG413 |
A | HOH1026 |
A | HOH1027 |
B | LYS20 |
B | PRO23 |
B | VAL24 |
B | TYR26 |
B | SER47 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 1PE B 463 |
Chain | Residue |
A | GLU158 |
A | TYR192 |
A | HIS333 |
A | GLY336 |
A | HOH714 |
A | HOH825 |
A | HOH875 |
A | HOH1003 |
B | LYS20 |
B | THR21 |
B | GLU22 |
B | PRO23 |
B | AES1474 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 464 |
Chain | Residue |
B | HIS156 |
B | ALA157 |
B | GLU189 |
B | THR247 |
B | ASP248 |
B | HOH482 |
B | HOH509 |
B | HOH510 |
B | HOH511 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 465 |
Chain | Residue |
A | ASP316 |
A | HOH802 |
A | HOH803 |
B | ARG334 |
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 |