3VX1
Crystal Structure of alpha-Amylase from Aspergillus oryzae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0009277 | cellular_component | fungal-type cell wall |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030287 | cellular_component | cell wall-bounded periplasmic space |
A | 0030428 | cellular_component | cell septum |
A | 0031521 | cellular_component | spitzenkorper |
A | 0032163 | cellular_component | hyphal septin band |
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:0000305|PubMed:9283074 |
Chain | Residue | Details |
A | ASP206 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:9283074 |
Chain | Residue | Details |
A | GLU230 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9283074 |
Chain | Residue | Details |
A | GLN35 | |
A | TRP83 | |
A | HIS122 | |
A | ARG204 | |
A | LYS209 | |
A | GLY234 | |
A | ASP297 | |
A | ARG344 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16880540, ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074 |
Chain | Residue | Details |
A | ASN121 | |
A | GLU162 | |
A | ASP175 | |
A | HIS210 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9283074 |
Chain | Residue | Details |
A | ASP206 | |
A | GLU230 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:9283074 |
Chain | Residue | Details |
A | ASP297 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16880540 |
Chain | Residue | Details |
A | ASN197 |