{"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"}}}