7CBB
Crystal structure of SbnC in the biosynthesis of staphyloferrin B
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016881 | molecular_function | acid-amino acid ligase activity |
| A | 0019290 | biological_process | siderophore biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016881 | molecular_function | acid-amino acid ligase activity |
| B | 0019290 | biological_process | siderophore biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue AMP A 601 |
| Chain | Residue |
| A | ASP146 |
| A | HOH709 |
| A | HOH742 |
| A | HOH764 |
| A | HOH769 |
| A | ARG147 |
| A | PRO148 |
| A | LYS156 |
| A | SER265 |
| A | ARG267 |
| A | ARG292 |
| A | HIS424 |
| A | GLN426 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue AMP B 601 |
| Chain | Residue |
| B | ASP146 |
| B | LYS156 |
| B | SER265 |
| B | ARG267 |
| B | SER287 |
| B | LEU288 |
| B | ARG292 |
| B | HIS424 |
| B | GLN426 |
| B | HOH702 |
| B | HOH706 |
| B | HOH772 |
| B | HOH801 |
