4HOX
The crystal structure of isomaltulose synthase from Erwinia rhapontici NX5 in complex with Tris
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000025 | biological_process | maltose catabolic process |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0004574 | molecular_function | oligo-1,6-glucosidase activity |
A | 0004575 | molecular_function | sucrose alpha-glucosidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005987 | biological_process | sucrose catabolic process |
A | 0006865 | biological_process | amino acid transport |
A | 0016853 | molecular_function | isomerase activity |
A | 0032450 | molecular_function | maltose alpha-glucosidase activity |
A | 0033934 | molecular_function | glucan 1,4-alpha-maltotriohydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRS A 701 |
Chain | Residue |
A | ASP102 |
A | HOH835 |
A | HOH844 |
A | TYR105 |
A | HIS145 |
A | PHE186 |
A | PHE205 |
A | ASP241 |
A | GLU295 |
A | ARG456 |
A | GOL702 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 702 |
Chain | Residue |
A | GLU295 |
A | ARG325 |
A | ASP369 |
A | GLU428 |
A | ARG456 |
A | TRS701 |
A | HOH1394 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 703 |
Chain | Residue |
A | ASP63 |
A | ASN65 |
A | ASP67 |
A | ILE69 |
A | ASP71 |
A | HOH1397 |
A | HOH1398 |