Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0035494 | biological_process | SNARE complex disassembly |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 99 |
Chain | Residue |
A | ANP1 |
A | HOH242 |
A | HOH243 |
A | HOH244 |
A | THR558 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ANP A 1 |
Chain | Residue |
A | HOH168 |
A | HOH241 |
A | HOH243 |
A | ILE511 |
A | MET512 |
A | ASN513 |
A | GLY514 |
A | ILE515 |
A | ILE516 |
A | TRP518 |
A | VAL522 |
A | PRO553 |
A | HIS554 |
A | SER555 |
A | GLY556 |
A | LYS557 |
A | THR558 |
A | ALA559 |
A | LEU560 |
A | LYS639 |
A | SER655 |
A | LYS716 |
A | MG99 |
A | HOH102 |
A | HOH120 |
A | HOH160 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 371 |
Chain | Residue |
A | GLU689 |
A | ASP696 |
A | THR700 |
A | THR700 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLY514 | |
A | HIS554 | |
Chain | Residue | Details |
A | ALA559 | |
Chain | Residue | Details |
A | PRO578 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
A | THR558 | electrostatic stabiliser |
A | ALA559 | electrostatic stabiliser |
A | ASP612 | electrostatic stabiliser |
A | ILE613 | proton acceptor |
A | LYS640 | electrostatic stabiliser |
A | LYS717 | electrostatic stabiliser |