5GTW
The N253R mutant structures of trehalose synthase from Deinococcus radiodurans display two different active-site conformations
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 | 5 |
| Details | binding site for residue CA A 601 |
| 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 602 |
| 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 603 |
| Chain | Residue |
| A | ASP63 |
| A | HIS106 |
| A | PHE151 |
| A | PHE173 |
| A | ASP209 |
| A | GLU251 |
| A | ARG253 |
| A | ARG398 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 601 |
| Chain | Residue |
| B | ASN105 |
| B | ASP179 |
| B | LEU180 |
| B | TYR213 |
| B | LEU214 |
| B | GLU216 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 602 |
| Chain | Residue |
| B | ASP24 |
| B | ASN26 |
| B | ASP28 |
| B | LYS30 |
| B | GLY31 |
| B | ASP32 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue TRS B 603 |
| 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 601 |
| Chain | Residue |
| C | ASN105 |
| C | ASP179 |
| C | LEU180 |
| C | TYR213 |
| C | LEU214 |
| C | GLU216 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 602 |
| 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 603 |
| 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 | 5 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | ASP24 |
| D | ASN26 |
| D | ASP28 |
| D | LYS30 |
| D | ASP32 |
