Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0015986 | biological_process | proton motive force-driven ATP synthesis |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0033178 | cellular_component | proton-transporting two-sector ATPase complex, catalytic domain |
A | 0046034 | biological_process | ATP metabolic process |
A | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE VO4 A 589 |
Chain | Residue |
A | PRO233 |
A | SER238 |
A | LYS240 |
A | THR241 |
A | LEU417 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE VO4 A 590 |
Chain | Residue |
A | PRO233 |
A | LEU417 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY A 591 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 592 |
Chain | Residue |
A | ILE184 |
A | LEU550 |
A | LEU582 |
A | HOH644 |
A | GLU183 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 593 |
Chain | Residue |
A | THR241 |
A | VAL242 |
A | THR243 |
A | PHE427 |
A | PRO428 |
A | ALA429 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 594 |
Chain | Residue |
A | GLN246 |
A | LYS249 |
A | ALA507 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 595 |
Chain | Residue |
A | ALA337 |
A | PRO402 |
A | VAL403 |
A | ASN406 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY A 596 |
Chain | Residue |
A | ASN431 |
A | TRP432 |
A | LEU433 |
A | HOH664 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 597 |
Chain | Residue |
A | LYS461 |
A | ASP532 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TRS A 598 |
Chain | Residue |
A | TRP250 |
A | GLU510 |
A | VAL511 |
A | TYR514 |
A | ARG563 |
A | HOH640 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY A 599 |
Chain | Residue |
A | GLY323 |
A | ASP325 |
A | VAL383 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY A 600 |
Chain | Residue |
A | ASN539 |
A | ARG553 |
A | GLU554 |
Functional Information from PROSITE/UniProt
site_id | PS00152 |
Number of Residues | 10 |
Details | ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINWLTSYS |
Chain | Residue | Details |
A | PRO428-SER437 | |