5JM8
The structure of ATP-bound aerobactin synthetase IucA from a hypervirulent pathotype of Klebsiella pneumoniae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016881 | molecular_function | acid-amino acid ligase activity |
| A | 0019290 | biological_process | siderophore biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016881 | molecular_function | acid-amino acid ligase activity |
| B | 0019290 | biological_process | siderophore biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016881 | molecular_function | acid-amino acid ligase activity |
| C | 0019290 | biological_process | siderophore biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016881 | molecular_function | acid-amino acid ligase activity |
| D | 0019290 | biological_process | siderophore biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016881 | molecular_function | acid-amino acid ligase activity |
| E | 0019290 | biological_process | siderophore biosynthetic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0016881 | molecular_function | acid-amino acid ligase activity |
| F | 0019290 | biological_process | siderophore biosynthetic process |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0016881 | molecular_function | acid-amino acid ligase activity |
| G | 0019290 | biological_process | siderophore biosynthetic process |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0016881 | molecular_function | acid-amino acid ligase activity |
| H | 0019290 | biological_process | siderophore biosynthetic process |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue ATP A 600 |
| Chain | Residue |
| A | LEU143 |
| A | ARG347 |
| A | VAL363 |
| A | HIS425 |
| A | GLN426 |
| A | GLN427 |
| A | ARG444 |
| A | ASP445 |
| A | ASN487 |
| A | MG601 |
| A | HOH715 |
| A | GLY146 |
| A | HOH719 |
| A | HOH756 |
| A | HIS147 |
| A | SER262 |
| A | ARG264 |
| A | SER265 |
| A | LYS276 |
| A | THR284 |
| A | ARG288 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | GLN427 |
| A | ASN428 |
| A | ASP445 |
| A | ATP600 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue ATP B 600 |
| Chain | Residue |
| B | LEU143 |
| B | GLY146 |
| B | HIS147 |
| B | SER262 |
| B | ARG264 |
| B | SER265 |
| B | LYS276 |
| B | THR284 |
| B | ARG288 |
| B | ARG347 |
| B | VAL363 |
| B | HIS425 |
| B | GLN426 |
| B | GLN427 |
| B | ASN428 |
| B | ASP445 |
| B | GLN447 |
| B | ASN487 |
| B | MG601 |
| B | HOH705 |
| B | HOH706 |
| B | HOH708 |
| B | HOH713 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | GLN427 |
| B | ASN428 |
| B | ASP445 |
| B | ATP600 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue ATP C 600 |
| Chain | Residue |
| C | LEU143 |
| C | GLY146 |
| C | HIS147 |
| C | SER262 |
| C | ARG264 |
| C | SER265 |
| C | LYS276 |
| C | THR284 |
| C | ARG288 |
| C | ARG347 |
| C | VAL363 |
| C | HIS425 |
| C | GLN426 |
| C | GLN427 |
| C | ASP445 |
| C | GLN447 |
| C | ASN487 |
| C | MG601 |
| C | HOH714 |
| C | HOH717 |
| C | HOH732 |
| C | HOH779 |
| C | HOH793 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | GLN427 |
| C | ASN428 |
| C | ASP445 |
| C | ATP600 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue ATP D 600 |
| Chain | Residue |
| D | HOH755 |
| D | LEU143 |
| D | GLY146 |
| D | HIS147 |
| D | SER262 |
| D | ARG264 |
| D | SER265 |
| D | LYS276 |
| D | THR284 |
| D | ARG288 |
| D | ARG347 |
| D | VAL363 |
| D | HIS425 |
| D | GLN426 |
| D | GLN427 |
| D | ASN428 |
| D | ASP445 |
| D | ASN487 |
| D | MG601 |
| D | HOH721 |
| D | HOH738 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | HIS425 |
| D | GLN427 |
| D | ASN428 |
| D | ASP445 |
| D | ATP600 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | binding site for residue ATP E 600 |
| Chain | Residue |
| E | GLY146 |
| E | HIS147 |
| E | SER262 |
| E | ARG264 |
| E | SER265 |
| E | LYS276 |
| E | THR284 |
| E | ARG288 |
| E | ARG347 |
| E | HIS425 |
| E | GLN427 |
| E | ASP445 |
| E | GLN447 |
| E | ASN487 |
| E | MG601 |
| E | HOH705 |
| E | HOH731 |
| E | HOH739 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | GLN427 |
| E | ASN428 |
| E | ASP445 |
| E | ATP600 |
| site_id | AD2 |
| Number of Residues | 18 |
| Details | binding site for residue ATP F 600 |
| Chain | Residue |
| F | LEU143 |
| F | HIS147 |
| F | SER262 |
| F | ARG264 |
| F | SER265 |
| F | LYS276 |
| F | LEU283 |
| F | THR284 |
| F | ARG288 |
| F | ARG347 |
| F | HIS425 |
| F | GLN427 |
| F | ASN428 |
| F | ASP445 |
| F | GLN447 |
| F | ASN487 |
| F | MG601 |
| F | HOH715 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG F 601 |
| Chain | Residue |
| F | GLN427 |
| F | ASN428 |
| F | ASP445 |
| F | ATP600 |
| site_id | AD4 |
| Number of Residues | 23 |
| Details | binding site for residue ATP G 600 |
| Chain | Residue |
| G | LEU143 |
| G | GLY146 |
| G | HIS147 |
| G | SER262 |
| G | ARG264 |
| G | SER265 |
| G | LYS276 |
| G | THR284 |
| G | ARG288 |
| G | ARG347 |
| G | VAL363 |
| G | HIS425 |
| G | GLN426 |
| G | GLN427 |
| G | ASN428 |
| G | ASP445 |
| G | ASN487 |
| G | MG601 |
| G | HOH716 |
| G | HOH732 |
| G | HOH736 |
| G | HOH761 |
| G | HOH767 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue MG G 601 |
| Chain | Residue |
| G | HIS425 |
| G | GLN427 |
| G | ASN428 |
| G | ASP445 |
| G | ATP600 |
| site_id | AD6 |
| Number of Residues | 23 |
| Details | binding site for residue ATP H 600 |
| Chain | Residue |
| H | LEU143 |
| H | GLY146 |
| H | HIS147 |
| H | SER262 |
| H | ARG264 |
| H | SER265 |
| H | LYS276 |
| H | THR284 |
| H | ARG288 |
| H | ARG347 |
| H | VAL363 |
| H | HIS425 |
| H | GLN426 |
| H | GLN427 |
| H | ASN428 |
| H | ASP445 |
| H | GLN447 |
| H | ASN487 |
| H | MG601 |
| H | HOH723 |
| H | HOH730 |
| H | HOH748 |
| H | HOH759 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue MG H 601 |
| Chain | Residue |
| H | HIS425 |
| H | GLN427 |
| H | ASN428 |
| H | ASP445 |
| H | ATP600 |
