4RM3
Crystal structure of a benzoate coenzyme A ligase with 2-Furoic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0016405 | molecular_function | CoA-ligase activity |
A | 0016874 | molecular_function | ligase activity |
A | 0016878 | molecular_function | acid-thiol ligase activity |
A | 0044550 | biological_process | secondary metabolite biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005524 | molecular_function | ATP binding |
B | 0016405 | molecular_function | CoA-ligase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0016878 | molecular_function | acid-thiol ligase activity |
B | 0044550 | biological_process | secondary metabolite biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FOA A 1000 |
Chain | Residue |
A | TYR228 |
A | ALA302 |
A | GLY303 |
A | GLY327 |
A | SER328 |
A | HIS333 |
A | ILE334 |
A | LYS427 |
A | HOH1308 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE FOA B 1000 |
Chain | Residue |
B | TYR228 |
B | ALA302 |
B | GLY303 |
B | ILE326 |
B | GLY327 |
B | SER328 |
B | HIS333 |
B | ILE334 |
B | LYS427 |
B | HOH1154 |
B | HOH1275 |