6M2U
The crystal structure of benzoate coenzyme A ligase double mutant (H333A/I334A) in complex with 2-chloro-1,3-thiazole-5-carboxylate-AMP
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 | 26 |
Details | binding site for residues AMP A 601 and F0O A 602 |
Chain | Residue |
A | TYR228 |
A | SER328 |
A | THR329 |
A | ALA333 |
A | ALA334 |
A | SER404 |
A | ASP406 |
A | ARG421 |
A | LYS427 |
A | TYR432 |
A | HOH724 |
A | ALA302 |
A | HOH727 |
A | HOH749 |
A | HOH818 |
A | HOH920 |
A | HOH944 |
A | HOH1076 |
A | HOH1200 |
A | GLY303 |
A | GLU304 |
A | ALA305 |
A | ASP324 |
A | GLY325 |
A | ILE326 |
A | GLY327 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residues AMP B 601 and F0O B 602 |
Chain | Residue |
B | TYR228 |
B | ALA302 |
B | GLY303 |
B | GLU304 |
B | ALA305 |
B | ASP324 |
B | GLY325 |
B | ILE326 |
B | GLY327 |
B | SER328 |
B | THR329 |
B | ALA333 |
B | ALA334 |
B | ASP406 |
B | ARG421 |
B | LYS427 |
B | TYR432 |
B | HOH722 |
B | HOH730 |
B | HOH815 |
B | HOH870 |
B | HOH887 |
B | HOH1044 |
B | HOH1070 |