5YKB
The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site conformation
Replaces: 5GTVFunctional 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 | 6 |
| Details | binding site for residue CA A 600 |
| Chain | Residue |
| A | ASN105 |
| A | ASP179 |
| A | LEU180 |
| A | TYR213 |
| A | LEU214 |
| A | GLU216 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | LYS30 |
| A | ASP32 |
| A | ASP24 |
| A | ASN26 |
| A | ASP28 |
| site_id | AC3 |
| 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 | AC4 |
| 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 | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 600 |
| Chain | Residue |
| C | ASN105 |
| C | ASP179 |
| C | TYR213 |
| C | LEU214 |
| C | GLU216 |
| site_id | AC6 |
| 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 | AC7 |
| 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 | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | ASP24 |
| D | ASN26 |
| D | ASP28 |
| D | LYS30 |
| D | ASP32 |
