1TMQ
STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031404 | molecular_function | chloride ion binding |
| A | 0043169 | molecular_function | cation binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1002 |
| Chain | Residue |
| A | ARG183 |
| A | LEU243 |
| A | ASN285 |
| A | ARG321 |
| A | HOH1067 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1001 |
| Chain | Residue |
| A | HOH1049 |
| A | HOH5011 |
| A | ASN98 |
| A | ARG146 |
| A | ASP155 |
| A | HIS189 |
Functional Information from PROSITE/UniProt
| site_id | PS00426 |
| Number of Residues | 24 |
| Details | CEREAL_TRYP_AMYL_INH Cereal trypsin/alpha-amylase inhibitors family signature. CipgmAiphnPLdsCRwYVstrtC |
| Chain | Residue | Details |
| B | CYS506-CYS529 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 17 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9600843","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9600843","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10508777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9600843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687373","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JAE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP185 | |
| A | GLY210 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP287 | |
| A | ASP185 | |
| A | GLU222 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1amy |
| Chain | Residue | Details |
| A | ASP287 | |
| A | ASP185 | |
| A | GLU229 |
