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
Chain | Residue | Details |
A | GLY502 | |
B | GLY502 | |
C | GLY502 | |
D | GLY502 | |