{"id":"d10e301d-a8c2-5547-82fb-cd2b9dac631f","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-aoc3-copper-tpq","predicate":"contains_catalytic","statement":"The human AOC3 structure contained an active-site copper ion and TPQ in its active off-copper conformation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"916dde92-0f83-5cd3-86b9-2c643688272c","mechanism_event_label":"A separate copper amine oxidase has its own catalytic arrangement.","subject":{"id":"cb297ed5-162d-5d7c-94e1-d5d5d9c49294","slug":"aoc3","display_name":"Human copper amine oxidase AOC3 / vascular adhesion protein 1 / VAP-1","entity_type_key":"protein"},"object":{"id":"6dd387e0-1f91-5bef-8e84-c7bfabce7e9a","slug":"topaquinone-cofactor","display_name":"Protein-derived topaquinone / TPQ cofactor","entity_type_key":"chemical_species"},"evidence_count":1,"mechanism_event":{"id":"916dde92-0f83-5cd3-86b9-2c643688272c","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-aoc3-copper-tpq-event","event_type":"biochemical_relationship","label":"A separate copper amine oxidase has its own catalytic arrangement.","description":"The human AOC3 structure contained an active-site copper ion and TPQ in its active off-copper conformation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9f0afdde-1ec1-5c8a-bb5e-f3b2b75f67f6","slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"},"role":"enzyme-bound metal","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"cb297ed5-162d-5d7c-94e1-d5d5d9c49294","slug":"aoc3","display_name":"Human copper amine oxidase AOC3 / vascular adhesion protein 1 / VAP-1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"6dd387e0-1f91-5bef-8e84-c7bfabce7e9a","slug":"topaquinone-cofactor","display_name":"Protein-derived topaquinone / TPQ cofactor","entity_type_key":"chemical_species"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/16239734.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b\", \"start_char\": 0, \"end_char\": 1408, \"text_sha256\": \"24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"X-ray structures of soluble human VAP-1 and inhibitor complex","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Native and inhibitor-bound structure","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Soluble protein structure; proposed gate and adhesion-motif functions are not proven clinical effects of copper intake.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Copper research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Human protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A separate copper amine oxidase has its own catalytic arrangement.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p16239734] Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. (2005). https://pubmed.ncbi.nlm.nih.gov/16239734/ DOI: 10.1107/s0907444905028805","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified truncated soluble AOC3","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"3d19f362-575a-5129-b2ba-61092e20aafa","evidence_kind":"source_excerpt","locator":"Lines 1040-1051","start_line":1040,"end_line":1051,"excerpt":"### copper-aoc3-copper-tpq\nThe human AOC3 structure contained an active-site copper ion and TPQ in its active off-copper conformation.\nCondition category: normal\nnutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A separate copper amine oxidase has its own catalytic arrangement.\norganism: Human protein\ntissue_or_cell_type: Purified truncated soluble AOC3\nexperimental_model: X-ray structures of soluble human VAP-1 and inhibitor complex\nlimitations: Soluble protein structure; proposed gate and adhesion-motif functions are not proven clinical effects of copper intake.\nexposure: Native and inhibitor-bound structure\nevidence_span: {\"source_cache\": \"artifacts/copper-research/16239734.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b\", \"start_char\": 0, \"end_char\": 1408, \"text_sha256\": \"24ea102446aeff31a53b9302d191c0bc572100f8ee82b6ccb1a665432151662b\"}\n[copper-p16239734] Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. 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