Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0035494 | biological_process | SNARE complex disassembly |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0035494 | biological_process | SNARE complex disassembly |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0035494 | biological_process | SNARE complex disassembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | ARG10 |
| A | CYS11 |
| A | PHE62 |
| A | ARG67 |
| A | HOH534 |
| A | HOH557 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| B | THR13 |
| B | HIS52 |
| B | HOH513 |
| B | HOH547 |
| C | HIS52 |
| A | THR13 |
| A | HIS52 |
| A | HOH506 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | ARG10 |
| B | CYS11 |
| B | PHE62 |
| B | ARG67 |
| B | HOH537 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 504 |
| Chain | Residue |
| C | ARG10 |
| C | CYS11 |
| C | ARG67 |
| C | HOH541 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | SER73 |
| A | ILE74 |
| A | HOH583 |
| A | HOH595 |
| B | LYS150 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 506 |
| Chain | Residue |
| A | LYS150 |
| B | ARG10 |
| B | ARG67 |
| B | HOH578 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 507 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 508 |
| Chain | Residue |
| C | SER73 |
| C | ILE74 |
| C | HOH560 |
| C | HOH573 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BME A 400 |
| Chain | Residue |
| A | CYS11 |
| A | PRO12 |
| A | LEU16 |
| A | SER17 |
| A | SER19 |
| A | CYS21 |
| A | VAL23 |
| A | ALA61 |
| A | PHE62 |
| A | SER63 |
| A | GLN66 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME A 401 |
| Chain | Residue |
| A | PHE85 |
| A | LYS87 |
| A | GLN90 |
| A | CYS91 |
| A | LEU176 |
| A | HOH517 |
| A | HOH596 |
| B | GLY179 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BME B 400 |
| Chain | Residue |
| B | CYS11 |
| B | PRO12 |
| B | LEU16 |
| B | SER17 |
| B | SER19 |
| B | CYS21 |
| B | VAL23 |
| B | ALA61 |
| B | PHE62 |
| B | SER63 |
| B | GLN66 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME B 401 |
| Chain | Residue |
| A | GLY179 |
| B | PHE85 |
| B | LYS87 |
| B | GLN90 |
| B | CYS91 |
| B | LEU176 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BME C 400 |
| Chain | Residue |
| C | CYS11 |
| C | PRO12 |
| C | LEU16 |
| C | SER17 |
| C | SER19 |
| C | CYS21 |
| C | VAL23 |
| C | ALA61 |
| C | PHE62 |
| C | SER63 |
| C | GLN66 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME C 401 |
| Chain | Residue |
| C | PHE85 |
| C | LYS87 |
| C | GLN90 |
| C | CYS91 |
| C | LEU176 |
| C | GLY179 |
| C | HOH525 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P46460","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 642 |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 642 |
| site_id | MCSA3 |
| Number of Residues | |
| Details | M-CSA 642 |
