2D3N
Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005983 | biological_process | starch catabolic process |
A | 0008152 | biological_process | metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0033927 | molecular_function | glucan 1,4-alpha-maltohexaosidase activity |
A | 0043169 | molecular_function | cation binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | ASP236 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU266 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00692 |
Chain | Residue | Details |
A | ASN106 | |
A | ASP163 | |
A | ALA186 | |
A | ASP188 | |
A | ASP199 | |
A | ASP205 | |
A | ASP207 | |
A | ASP209 | |
A | HIS240 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | ASP333 |