9MY5
Structure of the BasE mutant V336A, an NRPS adenylation domain in the acinetobactin biosynthetic pathway bound to 4-methyl salicylic Acid
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008668 | molecular_function | 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016878 | molecular_function | acid-thiol ligase activity |
| A | 0019290 | biological_process | siderophore biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008668 | molecular_function | 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016878 | molecular_function | acid-thiol ligase activity |
| B | 0019290 | biological_process | siderophore biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. FQLSGGSTGtPK |
| Chain | Residue | Details |
| B | PHE194-LYS205 |






