{"id":"f543bd1f-afc2-5cd2-a1a1-cffe7d971747","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-enz-glul-mn-crystals","predicate":"binds","statement":"Human GLUL crystal structures contained Mn with ADP/phosphate or ADP/phosphorylated methionine-sulfoximine.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"6d0f7816-6305-575c-966f-81dee00ac1b6","mechanism_event_label":"Human GLUL can bind manganese in the reported structural complexes.","subject":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"object":{"id":"d38cfc9c-9372-5e5f-8d91-03098155a3c6","slug":"glul","display_name":"Glutamine synthetase / GLUL","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"6d0f7816-6305-575c-966f-81dee00ac1b6","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-enz-glul-mn-crystals-event","event_type":"biochemical_relationship","label":"Human GLUL can bind manganese in the reported structural complexes.","description":"Human GLUL crystal structures contained Mn with ADP/phosphate or ADP/phosphorylated methionine-sulfoximine.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"d38cfc9c-9372-5e5f-8d91-03098155a3c6","slug":"glul","display_name":"Glutamine synthetase / GLUL","entity_type_key":"protein"},"role":"object","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"136c3764-1b93-5f79-8673-9001cab9bc3d","slug":"adp","display_name":"Adenosine diphosphate","entity_type_key":"small_molecule"},"role":"bound nucleotide","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Human GLUL ligand-complex crystal structures; canine apoenzyme comparison","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"ADP/phosphate/Mn and ADP/phosphorylated-inhibitor/Mn complexes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Crystallographic Mn binding does not establish exclusive Mn dependence or endogenous human brain metal occupancy.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Manganese research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"manganese","display_name":"Manganese","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Homo sapiens protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Human GLUL can bind manganese in the reported structural complexes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mn-enz-18005987] Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design. (2008). https://pubmed.ncbi.nlm.nih.gov/18005987/ DOI: 10.1016/j.jmb.2007.10.029","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified GLUL","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b6735dc3-bb18-5557-8637-60b9f6b680ff","evidence_kind":"source_excerpt","locator":"Lines 608-618","start_line":608,"end_line":618,"excerpt":"### mn-enz-glul-mn-crystals\nHuman GLUL crystal structures contained Mn with ADP/phosphate or ADP/phosphorylated methionine-sulfoximine.\nCondition category: normal\nnutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Human GLUL can bind manganese in the reported structural complexes.\norganism: Homo sapiens protein\ntissue_or_cell_type: Purified GLUL\nexperimental_model: Human GLUL ligand-complex crystal structures; canine apoenzyme comparison\nlimitations: Crystallographic Mn binding does not establish exclusive Mn dependence or endogenous human brain metal occupancy.\nexposure: ADP/phosphate/Mn and ADP/phosphorylated-inhibitor/Mn complexes\n[mn-enz-18005987] Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design. (2008). https://pubmed.ncbi.nlm.nih.gov/18005987/ DOI: 10.1016/j.jmb.2007.10.029","model_system":"Human GLUL ligand-complex crystal structures; canine apoenzyme comparison","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mn-enz-18005987] Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design. (2008). https://pubmed.ncbi.nlm.nih.gov/18005987/ DOI: 10.1016/j.jmb.2007.10.029","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"03224387-8a73-5b4f-906d-9f0be6625b7f","stable_key":"import-be889add-cec8-500b-be89-676431432a70","title":"Manganese: enzyme cofactors, glycosylation, transport 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":"f029ee5a1133a4f296047f06a6f0178deb9fd02e8d9707bc285bbe0f4e08fcb5","revision_id":"a77068c1-5a13-5aa9-bbac-d1cff6d34f15","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}