{"id":"e93d6e30-a128-5cac-9bb2-337dc438c682","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-dbh-copper-site-conformations","predicate":"has","statement":"Human DBH displayed open and closed active-site conformations; the closed structure placed its two copper-binding sites about 4–5 angstroms apart.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"925deaee-1696-5886-9526-0d695c6f5dea","mechanism_event_label":"The enzyme changes the spacing of its copper-binding regions; their precise catalytic cycle remains under study.","subject":{"id":"b1774c54-7759-53ce-bbc3-4663c7876d1d","slug":"dbh","display_name":"Human dopamine beta-hydroxylase / DBH","entity_type_key":"protein"},"object":{"id":"9f0afdde-1ec1-5c8a-bb5e-f3b2b75f67f6","slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"},"evidence_count":1,"mechanism_event":{"id":"925deaee-1696-5886-9526-0d695c6f5dea","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-dbh-copper-site-conformations-event","event_type":"biochemical_relationship","label":"The enzyme changes the spacing of its copper-binding regions; their precise catalytic cycle remains under study.","description":"Human DBH displayed open and closed active-site conformations; the closed structure placed its two copper-binding sites about 4–5 angstroms apart.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b1774c54-7759-53ce-bbc3-4663c7876d1d","slug":"dbh","display_name":"Human dopamine beta-hydroxylase / DBH","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"9f0afdde-1ec1-5c8a-bb5e-f3b2b75f67f6","slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/27152332.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09\", \"start_char\": 0, \"end_char\": 1325, \"text_sha256\": \"984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human DBH X-ray crystallography","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Crystal structure at 2.9 angstrom resolution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Open and closed conformations were observed; the proposed catalytic alternation and fully occupied binuclear states require further evidence. Do not equate a structural model with proof of psychiatric effects from 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":"The enzyme changes the spacing of its copper-binding regions; their precise catalytic cycle remains under study.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p27152332] The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution. (2016). https://pubmed.ncbi.nlm.nih.gov/27152332/ DOI: 10.1126/sciadv.1500980","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified dimeric enzyme","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"474d77da-f9be-5fcd-96cb-359ff5c5912f","evidence_kind":"source_excerpt","locator":"Lines 1092-1103","start_line":1092,"end_line":1103,"excerpt":"### copper-dbh-copper-site-conformations\nHuman DBH displayed open and closed active-site conformations; the closed structure placed its two copper-binding sites about 4–5 angstroms apart.\nCondition category: normal\nnutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The enzyme changes the spacing of its copper-binding regions; their precise catalytic cycle remains under study.\norganism: Human protein\ntissue_or_cell_type: Purified dimeric enzyme\nexperimental_model: Human DBH X-ray crystallography\nlimitations: Open and closed conformations were observed; the proposed catalytic alternation and fully occupied binuclear states require further evidence. Do not equate a structural model with proof of psychiatric effects from copper intake.\nexposure: Crystal structure at 2.9 angstrom resolution\nevidence_span: {\"source_cache\": \"artifacts/copper-research/27152332.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09\", \"start_char\": 0, \"end_char\": 1325, \"text_sha256\": \"984a9036d5157e29cdef55d42201887d3ff43cf533185148ba4e3f5c143ced09\"}\n[copper-p27152332] The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution. (2016). https://pubmed.ncbi.nlm.nih.gov/27152332/ DOI: 10.1126/sciadv.1500980","model_system":"Human DBH X-ray crystallography","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [copper-p27152332] The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution. (2016). https://pubmed.ncbi.nlm.nih.gov/27152332/ DOI: 10.1126/sciadv.1500980","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"9afba495-cbdc-51aa-998e-70a930dba3be","stable_key":"import-0ad8610d-d575-5870-b7cd-763a9f750783","title":"Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"84b0f62b2dae6835fa26902be87625c003c6c707492d3007e8f9d15420669008","revision_id":"d7e35b8b-3f77-56d9-90b5-5f542c63f321","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}