{"id":"20e3d487-e7b0-528f-925b-294bc10a20ae","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-trans-slc30a10-mn-coordination","predicate":"binds","statement":"The Mn-bound inward-facing human SLC30A10 cryo-EM structure placed Mn(II) at a site coordinated by D40, N127, D248 and S252.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"4da961ee-0bbf-5425-83d7-38238c0ba5f4","mechanism_event_label":"Four amino-acid residues form the transporter’s manganese-binding site.","subject":{"id":"5ba76eba-65ec-5f9c-a42d-dad58f6633d4","slug":"slc30a10","display_name":"Human manganese exporter SLC30A10","entity_type_key":"protein"},"object":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"evidence_count":1,"mechanism_event":{"id":"4da961ee-0bbf-5425-83d7-38238c0ba5f4","stable_key":"be889add-cec8-500b-be89-676431432a70:mn-trans-slc30a10-mn-coordination-event","event_type":"biochemical_relationship","label":"Four amino-acid residues form the transporter’s manganese-binding site.","description":"The Mn-bound inward-facing human SLC30A10 cryo-EM structure placed Mn(II) at a site coordinated by D40, N127, D248 and S252.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"a8082b11-c484-5792-bb81-48e8e699cbe4","slug":"manganese-ion","display_name":"Mn2+","entity_type_key":"ion"},"role":"transported_substrate","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"5ba76eba-65ec-5f9c-a42d-dad58f6633d4","slug":"slc30a10","display_name":"Human manganese exporter SLC30A10","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"false","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Cryo-EM of purified full-length human SLC30A10","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Purified full-length human SLC30A10 in Mn-bound and Mn-free cryo-EM preparations.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A resolved binding site supports molecular recognition; individual steps in the proposed conformational transport cycle remain a structural model.","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":"Human protein","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Four amino-acid residues form the transporter’s manganese-binding site.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mn-trans-41022720] Molecular mechanisms of SLC30A10-mediated manganese transport. (2025). https://pubmed.ncbi.nlm.nih.gov/41022720/ DOI: 10.1038/s41467-025-63616-7","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified membrane transporter","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"8b1db365-31f3-56e2-a506-86352564eba0","evidence_kind":"source_excerpt","locator":"Lines 383-394","start_line":383,"end_line":394,"excerpt":"### mn-trans-slc30a10-mn-coordination\nThe Mn-bound inward-facing human SLC30A10 cryo-EM structure placed Mn(II) at a site coordinated by D40, N127, D248 and S252.\nCondition category: normal\nnutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Four amino-acid residues form the transporter’s manganese-binding site.\norganism: Human protein\ntissue_or_cell_type: Purified membrane transporter\nexperimental_model: Cryo-EM of purified full-length human SLC30A10\nlimitations: A resolved binding site supports molecular recognition; individual steps in the proposed conformational transport cycle remain a structural model.\nexposure: Purified full-length human SLC30A10 in Mn-bound and Mn-free cryo-EM preparations.\ncross_nutrient: false\n[mn-trans-41022720] Molecular mechanisms of SLC30A10-mediated manganese transport. (2025). https://pubmed.ncbi.nlm.nih.gov/41022720/ DOI: 10.1038/s41467-025-63616-7","model_system":"Cryo-EM of purified full-length human SLC30A10","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mn-trans-41022720] Molecular mechanisms of SLC30A10-mediated manganese transport. (2025). https://pubmed.ncbi.nlm.nih.gov/41022720/ DOI: 10.1038/s41467-025-63616-7","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}