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 |