4TVU
Crystal structure of trehalose synthase from Deinococcus radiodurans reveals a closed conformation for catalysis of the intramolecular isomerization
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 |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0005975 | biological_process | carbohydrate metabolic process |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0005975 | biological_process | carbohydrate metabolic process |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0047471 | molecular_function | maltose alpha-D-glucosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 600 |
| Chain | Residue |
| A | ASN105 |
| A | ASP179 |
| A | TYR213 |
| A | LEU214 |
| A | GLU216 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | ASP32 |
| A | ASP24 |
| A | ASN26 |
| A | ASP28 |
| A | LYS30 |
| site_id | AC3 |
| Number of Residues | 8 |
| 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 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 600 |
| Chain | Residue |
| B | ASN105 |
| B | ASP179 |
| B | LEU180 |
| B | TYR213 |
| B | LEU214 |
| B | GLU216 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | ASP24 |
| B | ASN26 |
| B | ASP28 |
| B | LYS30 |
| B | ASP32 |
| site_id | AC6 |
| Number of Residues | 8 |
| 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 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 600 |
| Chain | Residue |
| C | ASN105 |
| C | ASP179 |
| C | TYR213 |
| C | LEU214 |
| C | GLU216 |
| C | HOH807 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | ASP24 |
| C | ASN26 |
| C | ASP28 |
| C | LYS30 |
| C | ASP32 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue TRS C 602 |
| Chain | Residue |
| C | ASP63 |
| C | TYR66 |
| C | HIS106 |
| C | PHE173 |
| C | ASP209 |
| C | GLU251 |
| C | ARG398 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 600 |
| Chain | Residue |
| D | ASN105 |
| D | ASP179 |
| D | TYR213 |
| D | LEU214 |
| D | GLU216 |
| site_id | AD2 |
| 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 | HOH797 |
| site_id | AD3 |
| Number of Residues | 8 |
| 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 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA E 600 |
| Chain | Residue |
| E | ASN105 |
| E | ASP179 |
| E | TYR213 |
| E | LEU214 |
| E | GLU216 |
| E | HOH893 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | ASP24 |
| E | ASN26 |
| E | ASP28 |
| E | LYS30 |
| E | ASP32 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue TRS E 602 |
| Chain | Residue |
| E | ASP63 |
| E | TYR66 |
| E | HIS106 |
| E | PHE173 |
| E | ASP209 |
| E | GLU251 |
| E | ARG398 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue CA F 600 |
| Chain | Residue |
| F | ASN105 |
| F | ASP179 |
| F | LEU180 |
| F | TYR213 |
| F | LEU214 |
| F | GLU216 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue MG F 601 |
| Chain | Residue |
| F | ASN26 |
| F | ASP28 |
| F | LYS30 |
| F | ASP32 |
| F | ASP24 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue TRS F 602 |
| Chain | Residue |
| F | ASP63 |
| F | TYR66 |
| F | HIS106 |
| F | PHE173 |
| F | ASP209 |
| F | GLU251 |
| F | ARG398 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue CA G 600 |
| Chain | Residue |
| G | ASN105 |
| G | ASP179 |
| G | TYR213 |
| G | LEU214 |
| G | GLU216 |
| G | HOH833 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue MG G 601 |
| Chain | Residue |
| G | ASP24 |
| G | ASN26 |
| G | ASP28 |
| G | LYS30 |
| G | ASP32 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue TRS G 602 |
| Chain | Residue |
| G | ASP63 |
| G | TYR66 |
| G | HIS106 |
| G | ASP209 |
| G | GLU251 |
| G | ARG398 |
| G | HOH828 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue CA H 600 |
| Chain | Residue |
| H | ASN105 |
| H | ASP179 |
| H | LEU180 |
| H | TYR213 |
| H | LEU214 |
| H | GLU216 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue MG H 601 |
| Chain | Residue |
| H | ASP24 |
| H | ASN26 |
| H | ASP28 |
| H | LYS30 |
| H | ASP32 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue TRS H 602 |
| Chain | Residue |
| H | ASP63 |
| H | TYR66 |
| H | HIS106 |
| H | PHE173 |
| H | ASP209 |
| H | GLU251 |
| H | ARG398 |
| H | HOH711 |
