{"metadata":{"accession":"PF07550","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR011432","hierarchy":null,"name":{"name":"Heme-binding protein Shr-like, Hb-interacting domain","short":"Shr-like_HID"},"description":[{"text":"<p>The Hb-interacting domain (HID) is found duplicated in Heme-binding protein Shr from Streptococcus pyogenes, a potentially lethal human pathogen, and in one to six copies in other uncharacterised bacterial proteins. Shr is a virulence factor that captures Hb and binds to the oxidized form of heme through an N-terminal region that contains two copies of this domain. HID shows a beta-sandwich-type fold in which two antiparallel beta-sheets are flanked by an alpha-helix [[cite:PUB00100888]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100888":{"PMID":30301765,"ISBN":null,"volume":"293","issue":"47","year":2018,"title":"The <i>Streptococcus pyogenes</i> Shr protein captures human hemoglobin using two structurally unique binding domains.","URL":null,"raw_pages":"18365-18377","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Macdonald R","Cascio D","Collazo MJ","Phillips M","Clubb RT."],"DOI_URL":null}},"set_info":{"accession":"CL0159","name":"E-set"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":250,"interactions":0,"matches":929,"pathways":0,"proteins":440,"proteomes":304,"sets":1,"structural_models":{"alphafold":157},"structures":4,"taxa":558},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":282,"alignment:full":618},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6dkq","name":"Crystal structure of the Shr Hemoglobin Interacting Domain 2"}}}