1AMY
CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005983 | biological_process | starch catabolic process |
| A | 0005987 | biological_process | sucrose catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 500 |
| Chain | Residue |
| A | GLY183 |
| A | HOH630 |
| A | ASN91 |
| A | ASP138 |
| A | ALA141 |
| A | ASP148 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | GLU108 |
| A | THR111 |
| A | ASP113 |
| A | ASP117 |
| A | HOH604 |
| A | HOH656 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | ASP127 |
| A | ASP142 |
| A | PHE143 |
| A | GLY144 |
| A | ALA146 |
| A | ASP148 |
| site_id | AS |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| A | ASP179 |
| A | GLU204 |
| A | ASP289 |
| site_id | SS |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| A | TRP276 |
| A | TRP277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8196040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634702","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AVA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00693","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9571044","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 8196040, 8535779 |
| Chain | Residue | Details |
| A | ASP179 | |
| A | GLU204 | |
| A | ASP289 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 397 |
| Chain | Residue | Details |
| A | ASP179 | covalent catalysis |
| A | GLU204 | hydrogen radical acceptor, proton shuttle (general acid/base) |
| A | ASP289 | electrostatic stabiliser, hydrogen radical acceptor, proton shuttle (general acid/base) |
