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{
    "metadata": {
        "accession": "IPR000833",
        "entry_id": null,
        "type": "family",
        "go_terms": [
            {
                "identifier": "GO:0015066",
                "name": "alpha-amylase inhibitor activity",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            }
        ],
        "source_database": "interpro",
        "member_databases": {
            "pirsf": {
                "PIRSF001658": "Alpha-amylase inhibitor, Streptomyces type"
            },
            "smart": {
                "SM00783": "Alpha amylase inhibitor"
            },
            "pfam": {
                "PF01356": "Alpha amylase inhibitor"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR000833",
            "name": "Alpha-amylase inhibitor",
            "type": "Family",
            "children": []
        },
        "name": {
            "name": "Alpha-amylase inhibitor",
            "short": "A-amylase_inhib"
        },
        "description": [
            {
                "text": "<p>Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor has no action on plant and microbial alpha amylases.</p>\r\n<p>A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases [[cite:PUB00027644]]. The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme.  The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00027644": {
                "PMID": 14501112,
                "ISBN": null,
                "volume": "59",
                "issue": "Pt 10",
                "year": 2003,
                "title": "Structure of the alpha-amylase inhibitor tendamistat at 0.93 A.",
                "URL": null,
                "raw_pages": "1737-43",
                "medline_journal": "Acta Crystallogr D Biol Crystallogr",
                "ISO_journal": "Acta Crystallogr. D Biol. Crystallogr.",
                "authors": [
                    "Konig V",
                    "Vertesy L",
                    "Schneider TR."
                ],
                "DOI_URL": "http://dx.doi.org/10.1107/S0907444903015828"
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR036379",
                "name": "Alpha-amylase inhibitor superfamily",
                "type": "homologous_superfamily"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 3,
            "interactions": 0,
            "matches": 582,
            "pathways": 0,
            "proteins": 582,
            "proteomes": 386,
            "sets": 0,
            "structural_models": {
                "alphafold": 316,
                "bfvd": 0
            },
            "structures": 7,
            "taxa": 589
        },
        "entry_annotations": {
            "alignment:seed": 48,
            "alignment:full": 209
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "1ok0",
            "name": "Crystal Structure of Tendamistat"
        }
    }
}