4WF7
Crystal structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in the intramolecular isomerization catalysis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 600 |
| Chain | Residue |
| A | ASN105 |
| A | ASP179 |
| A | TYR213 |
| A | LEU214 |
| A | GLU216 |
| A | HOH784 |
| A | HOH785 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | ASP28 |
| A | LYS30 |
| A | ASP32 |
| A | HOH833 |
| A | ASP24 |
| A | ASN26 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue TRS A 602 |
| Chain | Residue |
| A | ASP63 |
| A | TYR66 |
| A | HIS106 |
| A | PHE151 |
| A | PHE173 |
| A | ASP209 |
| A | GLU251 |
| A | ARG398 |
| A | HOH819 |
| A | HOH820 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue TRS A 603 |
| Chain | Residue |
| A | LEU61 |
| A | ARG62 |
| A | PHE174 |
| A | PRO396 |
| A | ASP397 |
| A | HOH894 |
| A | HOH902 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 600 |
| Chain | Residue |
| B | ASN105 |
| B | ASP179 |
| B | TYR213 |
| B | LEU214 |
| B | GLU216 |
| B | HOH788 |
| B | HOH865 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | ASP24 |
| B | ASN26 |
| B | ASP28 |
| B | LYS30 |
| B | ASP32 |
| B | HOH747 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue TRS B 602 |
| Chain | Residue |
| B | ASP63 |
| B | TYR66 |
| B | HIS106 |
| B | PHE151 |
| B | PHE173 |
| B | ASP209 |
| B | GLU251 |
| B | ARG398 |
| B | HOH785 |
| B | HOH855 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue CA C 600 |
| Chain | Residue |
| C | ASN105 |
| C | ASP179 |
| C | TYR213 |
| C | LEU214 |
| C | GLU216 |
| C | HOH743 |
| C | HOH845 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | ASP24 |
| C | ASN26 |
| C | ASP28 |
| C | LYS30 |
| C | ASP32 |
| C | HOH832 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue TRS C 602 |
| Chain | Residue |
| C | ASP63 |
| C | TYR66 |
| C | HIS106 |
| C | PHE151 |
| C | PHE173 |
| C | ASP209 |
| C | GLU251 |
| C | ARG398 |
| C | HOH811 |
| C | HOH816 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 600 |
| Chain | Residue |
| D | ASN105 |
| D | ASP179 |
| D | TYR213 |
| D | LEU214 |
| D | GLU216 |
| D | HOH839 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | ASP24 |
| D | ASN26 |
| D | ASP28 |
| D | LYS30 |
| D | ASP32 |
| D | HOH825 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue TRS D 602 |
| Chain | Residue |
| D | ASP63 |
| D | TYR66 |
| D | HIS106 |
| D | PHE151 |
| D | PHE173 |
| D | ASP209 |
| D | GLU251 |
| D | ARG398 |
| D | HOH813 |
| D | HOH931 |
