General Handler

HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept

{
    "metadata": {
        "accession": "IPR037110",
        "entry_id": null,
        "type": "homologous_superfamily",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "cathgene3d": {
                "G3DSA:2.102.20.10": "Beta-galactosidase, domain 2"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR037110",
            "name": "Beta-galactosidase, domain 2 superfamily",
            "type": "Homologous_superfamily",
            "children": []
        },
        "name": {
            "name": "Beta-galactosidase, domain 2 superfamily",
            "short": "Betagal_dom2_sf"
        },
        "description": [
            {
                "text": "<p>This entry represents the second domain of the five-domain beta-galactosidase enzyme that altogether catalyses the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and trans-glycosylation. This domain is made up of 16 antiparallel β-strands and an α-helix at its C terminus. The fold of this domain appears to be unique. In addition, the last seven strands of the domain form a subdomain with an immunoglobulin-like (I-type Ig) fold in which the first strand is divided between the two β-sheets. In penicillin spp this strand is interrupted by a 12-residue insertion which forms an additional edge-strand to the second β-sheet of the sub-domain. The remainder of the second domain forms a series of β-hairpins at its N terminus, four strands of which are contiguous with part of the Ig-like sub-domain, forming in total a seven-stranded antiparallel β-sheet.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": null,
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR018954",
                "name": "Beta-galactosidase, domain 2",
                "type": "domain"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 4616,
            "pathways": 1,
            "proteins": 4593,
            "proteomes": 1740,
            "sets": 0,
            "structural_models": {
                "alphafold": 3649,
                "bfvd": 0
            },
            "structures": 15,
            "taxa": 3445
        },
        "entry_annotations": {},
        "cross_references": {
            "ec": {
                "displayName": "ENZYME",
                "description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
                "rank": 19,
                "accessions": [
                    {
                        "accession": "3.2.1.23",
                        "url": "https://enzyme.expasy.org/EC/3.2.1.23"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}