Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 801 |
| Chain | Residue |
| A | HOH160 |
| A | HOH165 |
| A | HOH171 |
| A | SER509 |
| A | ATP800 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1801 |
| Chain | Residue |
| B | ATP1800 |
| B | HOH36 |
| B | HOH162 |
| B | HOH169 |
| B | SER509 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2801 |
| Chain | Residue |
| C | HOH137 |
| C | HOH148 |
| C | HOH166 |
| C | SER509 |
| C | ATP2800 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 3801 |
| Chain | Residue |
| D | HOH8 |
| D | HOH147 |
| D | HOH150 |
| D | SER509 |
| D | ATP3800 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP A 800 |
| Chain | Residue |
| A | HOH22 |
| A | HOH160 |
| A | HOH165 |
| A | HOH171 |
| A | TYR477 |
| A | ILE484 |
| A | SER504 |
| A | GLY505 |
| A | SER506 |
| A | GLY507 |
| A | LYS508 |
| A | SER509 |
| A | THR510 |
| A | MG801 |
| B | GLY605 |
| B | SER607 |
| B | GLY609 |
| B | GLN610 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP B 1800 |
| Chain | Residue |
| A | ALA604 |
| A | GLY605 |
| A | LEU606 |
| A | SER607 |
| A | GLY608 |
| A | GLY609 |
| A | GLN610 |
| B | HOH37 |
| B | HOH90 |
| B | HOH109 |
| B | HOH162 |
| B | HOH169 |
| B | TYR477 |
| B | ILE484 |
| B | SER504 |
| B | GLY505 |
| B | SER506 |
| B | GLY507 |
| B | LYS508 |
| B | SER509 |
| B | THR510 |
| B | MG1801 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP C 2800 |
| Chain | Residue |
| C | HOH51 |
| C | HOH137 |
| C | HOH148 |
| C | HOH166 |
| C | TYR477 |
| C | ILE484 |
| C | SER504 |
| C | GLY505 |
| C | SER506 |
| C | GLY507 |
| C | LYS508 |
| C | SER509 |
| C | THR510 |
| C | MG2801 |
| D | HOH118 |
| D | GLY605 |
| D | SER607 |
| D | GLY608 |
| D | GLY609 |
| D | GLN610 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP D 3800 |
| Chain | Residue |
| D | LYS513 |
| D | MG3801 |
| C | GLY605 |
| C | LEU606 |
| C | SER607 |
| C | GLY608 |
| C | GLY609 |
| C | GLN610 |
| D | HOH8 |
| D | HOH147 |
| D | HOH150 |
| D | HOH172 |
| D | TYR477 |
| D | ILE484 |
| D | SER504 |
| D | GLY505 |
| D | SER506 |
| D | GLY507 |
| D | LYS508 |
| D | SER509 |
| D | THR510 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRIAIARAL |
| Chain | Residue | Details |
| A | LEU606-LEU620 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 940 |
| Details | Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00362","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00362","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
