2GVY
Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution
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 | 0016787 | molecular_function | hydrolase activity |
| 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 |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009277 | cellular_component | fungal-type cell wall |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030287 | cellular_component | cell wall-bounded periplasmic space |
| B | 0030428 | cellular_component | cell septum |
| B | 0031521 | cellular_component | spitzenkorper |
| B | 0032163 | cellular_component | hyphal septin band |
| B | 0043169 | molecular_function | cation binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:9283074 |
| Chain | Residue | Details |
| A | ASP206 | |
| B | ASP206 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:9283074 |
| Chain | Residue | Details |
| A | GLU230 | |
| B | GLU230 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:9283074 |
| Chain | Residue | Details |
| A | GLN35 | |
| B | TRP83 | |
| B | HIS122 | |
| B | ARG204 | |
| B | LYS209 | |
| B | GLY234 | |
| B | ASP297 | |
| B | ARG344 | |
| A | TRP83 | |
| A | HIS122 | |
| A | ARG204 | |
| A | LYS209 | |
| A | GLY234 | |
| A | ASP297 | |
| A | ARG344 | |
| B | GLN35 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| 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 | |
| B | ASN121 | |
| B | GLU162 | |
| B | ASP175 | |
| B | HIS210 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9283074 |
| Chain | Residue | Details |
| A | ASP206 | |
| A | GLU230 | |
| B | ASP206 | |
| B | GLU230 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:9283074 |
| Chain | Residue | Details |
| A | ASP297 | |
| B | ASP297 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16880540 |
| Chain | Residue | Details |
| A | ASN197 | |
| B | ASN197 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP206 | |
| A | GLU230 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP206 | |
| B | GLU230 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | HIS122 | |
| A | ASP206 | |
| A | ASP297 | |
| A | GLU230 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | HIS122 | |
| B | ASP206 | |
| B | ASP297 | |
| B | GLU230 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP206 | |
| A | ASP297 | |
| A | GLU230 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ASP206 | |
| B | ASP297 | |
| B | GLU230 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ARG204 | |
| A | ASP206 | |
| A | HIS296 | |
| A | ASP297 | |
| A | GLU230 |
| site_id | CSA8 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| B | ARG204 | |
| B | ASP206 | |
| B | HIS296 | |
| B | ASP297 | |
| B | GLU230 |
