5ZLA
Crystal structure of mutant C387A of DFA-IIIase from Arthrobacter chlorophenolicus A6 in complex with DFA-III
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0033997 | molecular_function | inulin fructotransferase (DFA-I-forming) activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0033997 | molecular_function | inulin fructotransferase (DFA-I-forming) activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0033997 | molecular_function | inulin fructotransferase (DFA-I-forming) activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0033997 | molecular_function | inulin fructotransferase (DFA-I-forming) activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0033997 | molecular_function | inulin fructotransferase (DFA-I-forming) activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016829 | molecular_function | lyase activity |
| F | 0033997 | molecular_function | inulin fructotransferase (DFA-I-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue 9F3 A 501 |
| Chain | Residue |
| A | SER82 |
| A | GLN391 |
| A | HOH625 |
| A | HOH653 |
| A | HOH693 |
| D | ASP177 |
| D | ASP199 |
| D | ALA200 |
| D | GLN222 |
| D | HOH781 |
| A | SER84 |
| A | PHE207 |
| A | GLU210 |
| A | PHE256 |
| A | PRO257 |
| A | ARG258 |
| A | PHE281 |
| A | TRP309 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue 9F3 B 501 |
| Chain | Residue |
| A | ASP177 |
| A | ASP199 |
| A | ALA200 |
| A | HOH753 |
| B | PHE80 |
| B | SER82 |
| B | SER84 |
| B | PHE207 |
| B | GLU210 |
| B | PHE256 |
| B | PRO257 |
| B | ARG258 |
| B | PHE281 |
| B | TRP309 |
| B | GLN391 |
| B | HOH604 |
| B | HOH623 |
| B | HOH712 |
| B | HOH741 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue 9F3 C 501 |
| Chain | Residue |
| C | SER82 |
| C | SER84 |
| C | PHE207 |
| C | GLU210 |
| C | PHE256 |
| C | PRO257 |
| C | ARG258 |
| C | PHE281 |
| C | TRP309 |
| C | GLN391 |
| C | HOH611 |
| C | HOH660 |
| C | HOH700 |
| C | HOH731 |
| F | ASP177 |
| F | ASP199 |
| F | ALA200 |
| F | GLN222 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue 9F3 D 501 |
| Chain | Residue |
| B | ASP177 |
| B | ASP199 |
| B | ALA200 |
| B | GLN222 |
| D | PHE80 |
| D | SER82 |
| D | SER84 |
| D | PHE207 |
| D | GLU210 |
| D | PHE256 |
| D | PRO257 |
| D | ARG258 |
| D | PHE281 |
| D | TRP309 |
| D | GLN391 |
| D | HOH642 |
| D | HOH696 |
| D | HOH742 |
| D | HOH768 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue 9F3 E 501 |
| Chain | Residue |
| C | ASP177 |
| C | ASP199 |
| C | ALA200 |
| C | GLN222 |
| C | HOH687 |
| E | SER82 |
| E | SER84 |
| E | PHE207 |
| E | GLU210 |
| E | PHE256 |
| E | PRO257 |
| E | ARG258 |
| E | PHE281 |
| E | TRP309 |
| E | GLN391 |
| E | HOH619 |
| E | HOH680 |
| E | HOH744 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue 9F3 F 501 |
| Chain | Residue |
| F | GLU210 |
| F | PHE256 |
| F | PRO257 |
| F | ARG258 |
| F | PHE281 |
| F | TRP309 |
| F | GLN391 |
| F | HOH638 |
| F | HOH642 |
| F | HOH721 |
| F | HOH799 |
| E | ASP177 |
| E | ASP199 |
| E | ALA200 |
| E | GLN222 |
| F | SER82 |
| F | SER84 |
| F | PHE207 |
