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{
    "metadata": {
        "accession": "PF00905",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "pfam",
        "member_databases": null,
        "integrated": "IPR001460",
        "hierarchy": null,
        "name": {
            "name": "Penicillin binding protein transpeptidase domain",
            "short": "Transpeptidase"
        },
        "description": [
            {
                "text": "<p>The active site serine (residue 337 in [swissprot:P14677]) is conserved in all members of this family.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": [
            {
                "title": "Penicillin_binding_proteins",
                "extract": "<p><b>Penicillin-binding proteins</b> (<b>PBP</b>s) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of transpeptidase enzymes called <span><small>DD</small>-transpeptidases</span>.</p>",
                "thumbnail": null
            }
        ],
        "literature": {
            "PUB00003926": {
                "PMID": 8605631,
                "ISBN": null,
                "volume": "3",
                "issue": "3",
                "year": 1996,
                "title": "X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme.",
                "URL": null,
                "raw_pages": "284-9",
                "medline_journal": "Nat Struct Biol",
                "ISO_journal": "Nat. Struct. Biol.",
                "authors": [
                    "Pares S",
                    "Mouz N",
                    "Petillot Y",
                    "Hakenbeck R",
                    "Dideberg O."
                ],
                "DOI_URL": "http://dx.doi.org/10.1038/nsb0396-284"
            }
        },
        "set_info": {
            "accession": "CL0013",
            "name": "Beta-lactamase"
        },
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 209,
            "interactions": 0,
            "matches": 155242,
            "pathways": 0,
            "proteins": 154115,
            "proteomes": 17099,
            "sets": 1,
            "structural_models": {
                "alphafold": 117555,
                "bfvd": 0
            },
            "structures": 625,
            "taxa": 29909
        },
        "entry_annotations": {
            "hmm": 0,
            "logo": 0,
            "alignment:seed": 40,
            "alignment:full": 50114
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "7oda",
            "name": "OXA-48-like Beta-lactamase OXA-436"
        }
    }
}