1LWJ
CRYSTAL STRUCTURE OF T. MARITIMA 4-ALPHA-GLUCANOTRANSFERASE/ACARBOSE COMPLEX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004134 | molecular_function | 4-alpha-glucanotransferase activity |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009313 | biological_process | oligosaccharide catabolic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102500 | molecular_function | beta-maltose 4-alpha-glucanotransferase activity |
| B | 0004134 | molecular_function | 4-alpha-glucanotransferase activity |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009313 | biological_process | oligosaccharide catabolic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0043169 | molecular_function | cation binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0102500 | molecular_function | beta-maltose 4-alpha-glucanotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ACG B 988 |
| Chain | Residue |
| B | HOH36 |
| B | LYS630 |
| B | HIS631 |
| B | GLU657 |
| B | TRP659 |
| B | ALA660 |
| B | GLU661 |
| B | HIS718 |
| B | ASP719 |
| B | THR768 |
| B | TYR495 |
| B | HIS535 |
| B | GLU571 |
| B | TRP572 |
| B | PHE591 |
| B | ARG625 |
| B | ASP627 |
| B | ALA628 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ACG A 989 |
| Chain | Residue |
| A | HIS52 |
| A | TYR54 |
| A | HIS94 |
| A | TRP131 |
| A | PHE150 |
| A | ARG184 |
| A | ASP186 |
| A | ALA187 |
| A | LYS189 |
| A | HIS190 |
| A | GLU216 |
| A | TRP218 |
| A | HIS277 |
| A | ASP278 |
| A | THR327 |
| A | HOH1001 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 883 |
| Chain | Residue |
| A | ASP13 |
| A | ASN15 |
| A | ASP17 |
| A | VAL19 |
| A | ASP21 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 10 |
| Chain | Residue |
| B | ASP454 |
| B | ASN456 |
| B | ASP458 |
| B | VAL460 |
| B | ASP462 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | ASP186 | |
| B | ASP627 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | GLU216 | |
| B | GLU657 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP13 | |
| A | ASN15 | |
| A | ASP17 | |
| B | VAL460 | |
| B | ASP462 | |
| A | VAL19 | |
| A | ASP21 | |
| B | ASP454 | |
| B | ASN456 | |
| B | ASP458 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP278 | |
| B | ASP719 |
