1RP8
Crystal structure of barley alpha-amylase isozyme 1 (amy1) inactive mutant d180a in complex with maltoheptaose
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 | 0005983 | biological_process | starch catabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| 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:16030022, ECO:0000305|PubMed:7901200 |
| Chain | Residue | Details |
| A | ALA180 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:7901200 |
| Chain | Residue | Details |
| A | GLU205 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12906828 |
| Chain | Residue | Details |
| A | HIS45 | |
| A | ARG178 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16030022 |
| Chain | Residue | Details |
| A | ASN209 | |
| A | LYS271 | |
| A | HIS290 | |
| A | GLN296 | |
| A | TRP402 | |
| A | TYR52 | |
| A | TRP207 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12906828, ECO:0000269|PubMed:16030022, ECO:0000269|PubMed:17803687, ECO:0000269|PubMed:18588886 |
| Chain | Residue | Details |
| A | THR112 | |
| A | ASP114 | |
| A | ASP118 | |
| A | ASP128 | |
| A | ASP139 | |
| A | ALA142 | |
| A | ASP143 | |
| A | PHE144 | |
| A | ALA147 | |
| A | ASP149 | |
| A | GLY184 | |
| A | ASN92 | |
| A | GLU109 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12906828, ECO:0000305|PubMed:16030022 |
| Chain | Residue | Details |
| A | THR392 | |
| A | GLN227 | |
| A | GLY277 | |
| A | LYS375 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16030022, ECO:0000305|PubMed:17803687 |
| Chain | Residue | Details |
| A | ASP234 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12906828, ECO:0000305|PubMed:16030022, ECO:0000305|PubMed:17803687, ECO:0000305|PubMed:18588886 |
| Chain | Residue | Details |
| A | TYR380 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:7901200 |
| Chain | Residue | Details |
| A | ASP291 |
