1K1X
Crystal structure of 4-alpha-glucanotransferase from thermococcus litoralis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004134 | molecular_function | 4-alpha-glucanotransferase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0102500 | molecular_function | beta-maltose 4-alpha-glucanotransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004134 | molecular_function | 4-alpha-glucanotransferase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0102500 | molecular_function | beta-maltose 4-alpha-glucanotransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 1601 |
Chain | Residue |
A | ASP392 |
A | ASP394 |
A | ASP396 |
A | ARG398 |
A | GLU400 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 1602 |
Chain | Residue |
B | GLU400 |
B | ASP392 |
B | ASP394 |
B | ASP396 |
B | ARG398 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 1603 |
Chain | Residue |
A | ASN248 |
B | GLU60 |
B | HOH1668 |
B | HOH1681 |
B | HOH1759 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRS B 1604 |
Chain | Residue |
B | HIS11 |
B | GLU123 |
B | ASP214 |
B | TRP357 |
B | HOH1648 |
B | HOH1663 |
B | HOH1745 |
B | HOH1808 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | GLU123 | |
B | GLU123 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | ASP214 | |
B | ASP214 |