{"metadata":{"accession":"PF06452","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010502","hierarchy":null,"name":{"name":"Carbohydrate family 9 binding domain-like","short":"CBM9_1"},"description":[{"text":"<p>CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members.  The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerisation. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar [[cite:PUB00011788]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00011788":{"PMID":11371186,"ISBN":null,"volume":"40","issue":"21","year":2001,"title":"Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms.","URL":null,"raw_pages":"6248-56","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Notenboom V","Boraston AB","Kilburn DG","Rose DR."],"DOI_URL":"http://dx.doi.org/10.1021/bi0101704"}},"set_info":{"accession":"CL0559","name":"CBD9-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":503,"interactions":0,"matches":6400,"pathways":0,"proteins":6161,"proteomes":3332,"sets":1,"structural_models":{"alphafold":3453},"structures":7,"taxa":5255},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":16,"alignment:full":3264},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1i82","name":"FAMILY 9 CARBOHYDRATE-BINDING MODULE FROM THERMOTOGA MARITIMA XYLANASE 10A WITH CELLOBIOSE"}}}