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 | 3 |
Details | BINDING SITE FOR RESIDUE MG B 674 |
Chain | Residue |
B | ANP202 |
B | THR465 |
B | GLN493 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 674 |
Chain | Residue |
C | HOH38 |
C | HOH129 |
C | ANP203 |
C | THR465 |
C | GLN493 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 674 |
Chain | Residue |
A | THR465 |
A | GLN493 |
A | ANP201 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 674 |
Chain | Residue |
D | HOH6 |
D | ANP204 |
D | THR465 |
D | GLN493 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ANP A 201 |
Chain | Residue |
A | TRP401 |
A | LEU409 |
A | PHE430 |
A | THR460 |
A | GLY461 |
A | SER462 |
A | GLY463 |
A | LYS464 |
A | THR465 |
A | SER466 |
A | GLN493 |
A | MG674 |
B | MET498 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ANP B 202 |
Chain | Residue |
A | MET498 |
B | VAL428 |
B | THR460 |
B | GLY461 |
B | SER462 |
B | GLY463 |
B | LYS464 |
B | THR465 |
B | SER466 |
B | GLN493 |
B | MG674 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ANP C 203 |
Chain | Residue |
C | HOH38 |
C | PHE430 |
C | THR460 |
C | GLY461 |
C | SER462 |
C | GLY463 |
C | LYS464 |
C | THR465 |
C | SER466 |
C | GLN493 |
C | MET498 |
C | MG674 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ANP D 204 |
Chain | Residue |
D | HOH6 |
D | TRP401 |
D | PHE430 |
D | THR460 |
D | GLY461 |
D | SER462 |
D | GLY463 |
D | LYS464 |
D | THR465 |
D | SER466 |
D | GLN493 |
D | MET498 |
D | MG674 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 301 |
Chain | Residue |
A | LEU541 |
A | GLY542 |
A | GLY545 |
A | VAL546 |
A | THR547 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY B 302 |
Chain | Residue |
A | LEU578 |
B | HOH99 |
B | GLY542 |
B | GLY545 |
B | VAL546 |
B | THR547 |
B | LEU548 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY C 303 |
Chain | Residue |
C | HOH66 |
C | LEU541 |
C | GLY542 |
C | GLY545 |
C | VAL546 |
C | THR547 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY D 304 |
Chain | Residue |
D | LEU541 |
D | GLY542 |
D | GLY545 |
D | VAL546 |
D | THR547 |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV |
Chain | Residue | Details |
A | LEU548-VAL562 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | TRP401 | |
B | TRP401 | |
C | TRP401 | |
D | TRP401 | |
Chain | Residue | Details |
A | GLY458 | |
B | GLY458 | |
C | GLY458 | |
D | GLY458 | |
Chain | Residue | Details |
A | GLN493 | |
B | GLN493 | |
C | GLN493 | |
D | GLN493 | |
Chain | Residue | Details |
A | SER549 | |
A | SER660 | |
B | SER549 | |
B | SER660 | |
C | SER549 | |
C | SER660 | |
D | SER549 | |
D | SER660 | |
Chain | Residue | Details |
A | SER670 | |
B | SER670 | |
C | SER670 | |
D | SER670 | |
Chain | Residue | Details |
A | CYS524 | |
B | CYS524 | |
C | CYS524 | |
D | CYS524 | |