{"id":"11629fb5-ff7c-5648-8c38-e14d3d347759","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-aox-g1269r","predicate":"lacks_bound","statement":"The inactive AOX1 G1269R crystal structure lacked the entire Moco cofactor.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"52fbb687-655e-5b4c-9653-696e7ed3948a","mechanism_event_label":"Protein presence alone did not guarantee a working enzyme.","subject":{"id":"b826a2cd-368f-573d-a8a8-a157f10bc3c2","slug":"aox1-g1269r","display_name":"Human AOX1 p.Gly1269Arg","entity_type_key":"protein_state"},"object":{"id":"ac4bcc03-66fb-52c1-b191-9ecb2124659f","slug":"molybdenum-cofactor","display_name":"Molybdenum cofactor / Moco","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"52fbb687-655e-5b4c-9653-696e7ed3948a","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-aox-g1269r-event","event_type":"biochemical_relationship","label":"Protein presence alone did not guarantee a working enzyme.","description":"The inactive AOX1 G1269R crystal structure lacked the entire Moco cofactor.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b826a2cd-368f-573d-a8a8-a157f10bc3c2","slug":"aox1-g1269r","display_name":"Human AOX1 p.Gly1269Arg","entity_type_key":"protein_state"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ac4bcc03-66fb-52c1-b191-9ecb2124659f","slug":"molybdenum-cofactor","display_name":"Molybdenum cofactor / Moco","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/molybdenum-research/30985987.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0\", \"start_char\": 0, \"end_char\": 1497, \"text_sha256\": \"5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human AOX1 variant crystallography and CD/ThermoFAD stability assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Wild type compared with SNP variants","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"In-vitro structures and thermal stability; not physiological temperature or diet thresholds.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Molybdenum research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"molybdenum","display_name":"Molybdenum","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Protein presence alone did not guarantee a working enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified AOX1","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"03a2d316-437c-5f97-a9bd-993eca3d2a5b","evidence_kind":"source_excerpt","locator":"Lines 872-883","start_line":872,"end_line":883,"excerpt":"### mo-aox-g1269r\nThe inactive AOX1 G1269R crystal structure lacked the entire Moco cofactor.\nCondition category: machinery_impairment\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Protein presence alone did not guarantee a working enzyme.\norganism: Homo sapiens protein\ntissue_or_cell_type: Purified AOX1\nexperimental_model: Human AOX1 variant crystallography and CD/ThermoFAD stability assays\nlimitations: In-vitro structures and thermal stability; not physiological temperature or diet thresholds.\nexposure: Wild type compared with SNP variants\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/30985987.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0\", \"start_char\": 0, \"end_char\": 1497, \"text_sha256\": \"5442ecc25ebcf48ef56cc840357bfe9f233c2c9738d5e6b685db86aed2249fe0\"}\n[mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. 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