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 859 |
Chain | Residue |
A | THR550 |
A | ATP858 |
A | HOH889 |
A | HOH890 |
A | HOH891 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ATP A 858 |
Chain | Residue |
A | ILE508 |
A | VAL514 |
A | PRO545 |
A | HIS546 |
A | SER547 |
A | GLY548 |
A | LYS549 |
A | THR550 |
A | ALA551 |
A | LEU552 |
A | LYS631 |
A | SER647 |
A | ILE707 |
A | LYS708 |
A | LEU711 |
A | MG859 |
A | HOH863 |
A | HOH889 |
A | HOH890 |
A | HOH903 |
A | HOH919 |
A | HOH931 |
A | HOH959 |
A | ILE503 |
A | ASN505 |
A | GLY506 |
A | ILE507 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN505 | |
A | PRO545 | |
Chain | Residue | Details |
A | THR550 | |
Chain | Residue | Details |
A | SER569 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 642 |
Chain | Residue | Details |
A | LYS549 | electrostatic stabiliser |
A | THR550 | electrostatic stabiliser |
A | ASP603 | electrostatic stabiliser |
A | ASP604 | proton acceptor |
A | LYS631 | electrostatic stabiliser |
A | LYS708 | electrostatic stabiliser |