{"id":"c00daa15-cf57-59b9-ba7b-4c5b37671b47","stable_key":"1310afbd-6010-586e-805d-551d846da421:b6-met-scly-structure","predicate":"forms-binding-site-for","statement":"Human SCLY has two cofactor-containing active sites at its homodimer interface, with both subunits contributing to each site.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"b9687cd6-b97a-5f46-97a8-f09705c2597d","mechanism_event_label":"The selenium enzyme has a shared B6-binding architecture.","subject":{"id":"7c1bfe9f-559b-598e-9cca-8d0b032919fd","slug":"scly","display_name":"SCLY","entity_type_key":"protein"},"object":{"id":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"b9687cd6-b97a-5f46-97a8-f09705c2597d","stable_key":"1310afbd-6010-586e-805d-551d846da421:b6-met-scly-structure-event","event_type":"biochemical_relationship","label":"The selenium enzyme has a shared B6-binding architecture.","description":"Human SCLY has two cofactor-containing active sites at its homodimer interface, with both subunits contributing to each site.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"7c1bfe9f-559b-598e-9cca-8d0b032919fd","slug":"scly","display_name":"SCLY","entity_type_key":"protein"},"role":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"6b656ff5-9532-5da4-8eea-8ca163a48649","slug":"pyridoxal-phosphate","display_name":"PLP","entity_type_key":"small_molecule"},"role":"cofactor","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"B6-dependent machinery participates in selenium metabolism.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"existing_related_claim_ids","value_text":"[\"54d5691e-ef60-5f20-a204-abc3fcef9c21\", \"b6605dbc-466c-5591-965b-0a11b1b3c6fc\"]","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant human SCLY; structures and substrate assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Structural/biochemical evidence; dietary B6 withdrawal was not tested.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vitamin-b6","display_name":"Vitamin B6","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The selenium enzyme has a shared B6-binding architecture.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[b6-scly-2012] Biochemical Discrimination between Selenium and Sulfur 1: A Single Residue Provides Selenium Specificity to Human Selenocysteine Lyase (2012). https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0030581 DOI: 10.1371/journal.pone.0030581","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified recombinant protein; no intact tissue","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"44441050-905d-5f0d-9844-5815f71c080c","evidence_kind":"source_excerpt","locator":"Lines 924-935","start_line":924,"end_line":935,"excerpt":"### b6-met-scly-structure\nHuman SCLY has two cofactor-containing active sites at its homodimer interface, with both subunits contributing to each site.\nCondition category: normal\nnutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The selenium enzyme has a shared B6-binding architecture.\norganism: Homo sapiens\ntissue_or_cell_type: Purified recombinant protein; no intact tissue\nexperimental_model: Recombinant human SCLY; structures and substrate assays\nlimitations: Structural/biochemical evidence; dietary B6 withdrawal was not tested.\ncross_nutrient: B6-dependent machinery participates in selenium metabolism.\nexisting_related_claim_ids: [\"54d5691e-ef60-5f20-a204-abc3fcef9c21\", \"b6605dbc-466c-5591-965b-0a11b1b3c6fc\"]\n[b6-scly-2012] Biochemical Discrimination between Selenium and Sulfur 1: A Single Residue Provides Selenium Specificity to Human Selenocysteine Lyase (2012). https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0030581 DOI: 10.1371/journal.pone.0030581","model_system":"Recombinant human SCLY; structures and substrate assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [b6-scly-2012] Biochemical Discrimination between Selenium and Sulfur 1: A Single Residue Provides Selenium Specificity to Human Selenocysteine Lyase (2012). https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0030581 DOI: 10.1371/journal.pone.0030581","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"251773bb-16f5-5903-b135-db4a61d9dec4","stable_key":"import-1310afbd-6010-586e-805d-551d846da421","title":"Vitamin B6: mechanisms, deficiency 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":"ef0019b344b2219220f801a84d0d138ff6880c1be1a59540d9034bfa4334f61e","revision_id":"cac3555f-48af-5c52-a84e-add4482c87fb","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}