3KVZ
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase FlK - wild type FlK in complex with FAcCPan
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 |
| E | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0042803 | molecular_function | protein homodimerization activity |
| F | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0042803 | molecular_function | protein homodimerization activity |
| G | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0042803 | molecular_function | protein homodimerization activity |
| H | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ENV B 201 |
| Chain | Residue |
| A | GLU50 |
| B | GLY43 |
| B | HIS76 |
| B | ALA79 |
| A | LEU68 |
| A | GLY69 |
| A | HOH166 |
| B | VAL23 |
| B | LEU26 |
| B | VAL39 |
| B | ALA41 |
| B | THR42 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ENV E 202 |
| Chain | Residue |
| E | GLU50 |
| E | LEU68 |
| E | GLY69 |
| E | HOH348 |
| E | HOH689 |
| F | VAL23 |
| F | LEU26 |
| F | PHE33 |
| F | VAL39 |
| F | ALA41 |
| F | THR42 |
| F | GLY43 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | THR42 | |
| D | THR42 | |
| D | GLU50 | |
| D | HIS76 | |
| E | THR42 | |
| E | GLU50 | |
| E | HIS76 | |
| F | THR42 | |
| F | GLU50 | |
| F | HIS76 | |
| G | THR42 | |
| A | GLU50 | |
| G | GLU50 | |
| G | HIS76 | |
| H | THR42 | |
| H | GLU50 | |
| H | HIS76 | |
| A | HIS76 | |
| B | THR42 | |
| B | GLU50 | |
| B | HIS76 | |
| C | THR42 | |
| C | GLU50 | |
| C | HIS76 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE40 | |
| E | HIS76 | |
| F | PHE40 | |
| F | HIS76 | |
| G | PHE40 | |
| G | HIS76 | |
| H | PHE40 | |
| H | HIS76 | |
| A | HIS76 | |
| B | PHE40 | |
| B | HIS76 | |
| C | PHE40 | |
| C | HIS76 | |
| D | PHE40 | |
| D | HIS76 | |
| E | PHE40 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20430898, ECO:0000269|PubMed:20836570 |
| Chain | Residue | Details |
| A | GLY69 | |
| E | ARG120 | |
| F | GLY69 | |
| F | ARG120 | |
| G | GLY69 | |
| G | ARG120 | |
| H | GLY69 | |
| H | ARG120 | |
| A | ARG120 | |
| B | GLY69 | |
| B | ARG120 | |
| C | GLY69 | |
| C | ARG120 | |
| D | GLY69 | |
| D | ARG120 | |
| E | GLY69 |
