1L5A
Crystal Structure of VibH, an NRPS Condensation Enzyme
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0016880 | molecular_function | acid-ammonia (or amide) ligase activity |
A | 0019290 | biological_process | siderophore biosynthetic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0016880 | molecular_function | acid-ammonia (or amide) ligase activity |
B | 0019290 | biological_process | siderophore biosynthetic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0016880 | molecular_function | acid-ammonia (or amide) ligase activity |
C | 0019290 | biological_process | siderophore biosynthetic process |
Functional Information from PROSITE/UniProt
site_id | PS00591 |
Number of Residues | 11 |
Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. ALHLtVSEIDL |
Chain | Residue | Details |
A | ALA41-LEU51 |