3KVU
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA FlK - T42S mutant in complex with Acetyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACO A 201 |
| Chain | Residue |
| A | VAL23 |
| B | GLY69 |
| A | ALA41 |
| A | SER42 |
| A | HIS76 |
| A | THR77 |
| A | ALA78 |
| A | ALA79 |
| A | HOH414 |
| B | GLU50 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ACO B 200 |
| Chain | Residue |
| A | GLU50 |
| A | GLY69 |
| A | ALA121 |
| A | ILE123 |
| A | LYS127 |
| A | PHE128 |
| A | LYS131 |
| B | VAL23 |
| B | VAL39 |
| B | PHE40 |
| B | ALA41 |
| B | SER42 |
| B | HIS76 |
| B | THR77 |
| B | ALA78 |
| B | ALA79 |
| B | ASP111 |
| B | HOH365 |
| B | HOH453 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ACO D 202 |
| Chain | Residue |
| C | GLU50 |
| C | LEU68 |
| C | GLY69 |
| C | ARG99 |
| C | ALA121 |
| D | SER42 |
| D | HIS76 |
| D | THR77 |
| D | ALA78 |
| D | ALA79 |
| D | HOH405 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | SER42 | |
| A | GLU50 | |
| A | HIS76 | |
| B | SER42 | |
| B | GLU50 | |
| B | HIS76 | |
| C | SER42 | |
| C | GLU50 | |
| C | HIS76 | |
| D | SER42 | |
| D | GLU50 | |
| D | HIS76 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | PHE40 | |
| C | HIS76 | |
| D | PHE40 | |
| D | HIS76 | |
| A | PHE40 | |
| A | HIS76 | |
| B | PHE40 | |
| B | HIS76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20430898, ECO:0000269|PubMed:20836570 |
| Chain | Residue | Details |
| C | GLY69 | |
| C | ARG120 | |
| D | GLY69 | |
| D | ARG120 | |
| A | GLY69 | |
| A | ARG120 | |
| B | GLY69 | |
| B | ARG120 |
