{"id":"da6f4663-3be1-5949-8960-03cfce893eea","stable_key":"44737fa3-b335-53f4-a644-b9878d4416ac:creatine-ck-magnesium-complex","predicate":"coordinates","statement":"Magnesium in the transition-state analogue complex coordinated ADP, nitrate and water ligands at the creatine kinase active site.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"7253d7c8-bf70-5e67-b901-4004633a0a75","mechanism_event_label":"Magnesium helps position the phosphate-transfer chemistry; creatine is only one component of that reaction.","subject":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"object":{"id":"62d19e4d-a214-59b9-8272-0dec38a5fca5","slug":"ck-magnesium-transition-complex","display_name":"Magnesium-coordinated creatine kinase transition-state analogue complex","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"7253d7c8-bf70-5e67-b901-4004633a0a75","stable_key":"44737fa3-b335-53f4-a644-b9878d4416ac:creatine-ck-magnesium-complex-event","event_type":"biochemical_relationship","label":"Magnesium helps position the phosphate-transfer chemistry; creatine is only one component of that reaction.","description":"Magnesium in the transition-state analogue complex coordinated ADP, nitrate and water ligands at the creatine kinase active site.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e91848e3-1d6e-5c5a-8ae9-4e3fd7cb8dc9","slug":"torpedo-creatine-kinase","display_name":"Torpedo californica creatine kinase","entity_type_key":"protein"},"role":"enzyme","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"136c3764-1b93-5f79-8673-9001cab9bc3d","slug":"adp","display_name":"Adenosine diphosphate","entity_type_key":"small_molecule"},"role":"ligand","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"9f5df558-ed3d-5cda-b5ca-0f90f7aa6a8c","slug":"creatine","display_name":"Creatine","entity_type_key":"small_molecule"},"role":"substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"bff427ab-35f9-59c2-bb24-fd5953bbaec2","slug":"magnesium-ion","display_name":"Mg2+","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"62d19e4d-a214-59b9-8272-0dec38a5fca5","slug":"ck-magnesium-transition-complex","display_name":"Magnesium-coordinated creatine kinase transition-state analogue complex","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/creatine-research/12437342.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"291edd82015566452fe1b1321454a1df644a4c6da705fda90e8e369ea6ab53a1\", \"start_char\": 0, \"end_char\": 1625, \"text_sha256\": \"291edd82015566452fe1b1321454a1df644a4c6da705fda90e8e369ea6ab53a1\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"X-ray structure of a creatine kinase transition-state analogue complex","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"ADP, magnesium, nitrate and creatine complex at 2.1 angstrom resolution","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Nitrate models the transferring phosphoryl group; it is not declared a physiological substrate. Structural magnesium dependence does not establish benefit from extra oral magnesium.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Creatine research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"creatine","display_name":"Creatine","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Torpedo californica enzyme","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Magnesium helps position the phosphate-transfer chemistry; creatine is only one component of that reaction.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[creatine-p12437342] The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex. (2002). https://pubmed.ncbi.nlm.nih.gov/12437342/ DOI: 10.1021/bi026655p","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified creatine kinase","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"cccb830f-b664-532d-909c-02dd02bb66fa","evidence_kind":"source_excerpt","locator":"Lines 347-358","start_line":347,"end_line":358,"excerpt":"### creatine-ck-magnesium-complex\nMagnesium in the transition-state analogue complex coordinated ADP, nitrate and water ligands at the creatine kinase active site.\nCondition category: normal\nnutrient_topic: Creatine research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Magnesium helps position the phosphate-transfer chemistry; creatine is only one component of that reaction.\norganism: Torpedo californica enzyme\ntissue_or_cell_type: Purified creatine kinase\nexperimental_model: X-ray structure of a creatine kinase transition-state analogue complex\nlimitations: Nitrate models the transferring phosphoryl group; it is not declared a physiological substrate. Structural magnesium dependence does not establish benefit from extra oral magnesium.\nexposure: ADP, magnesium, nitrate and creatine complex at 2.1 angstrom resolution\nevidence_span: {\"source_cache\": \"artifacts/creatine-research/12437342.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"291edd82015566452fe1b1321454a1df644a4c6da705fda90e8e369ea6ab53a1\", \"start_char\": 0, \"end_char\": 1625, \"text_sha256\": \"291edd82015566452fe1b1321454a1df644a4c6da705fda90e8e369ea6ab53a1\"}\n[creatine-p12437342] The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex. (2002). https://pubmed.ncbi.nlm.nih.gov/12437342/ DOI: 10.1021/bi026655p","model_system":"X-ray structure of a creatine kinase transition-state analogue complex","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [creatine-p12437342] The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex. (2002). https://pubmed.ncbi.nlm.nih.gov/12437342/ DOI: 10.1021/bi026655p","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"70358046-c5c3-5e9a-9fc9-eb01c3fff88b","stable_key":"import-44737fa3-b335-53f4-a644-b9878d4416ac","title":"Creatine: synthesis, transport, phosphocreatine energetics 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. 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