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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]].","domain_architectures":503,"interpro_id":"IPR010502","known_evidence_count":null,"matches":6400,"name":"Carbohydrate family 9 binding domain-like","partial_evidence_count":null,"pfam_id":"PF06452","proteins":6161,"proteomes":3332,"short_name":"CBM9_1","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06452","structures":7,"taxa":5255,"unknown_status":"EX_DUF"},"inputs":{"cross_mech":"cross-mech-duf-examples-2026-10-10","members":"pfam-uniprot-uniref90-2026-10-07","protein_examples":"duf-protein-examples-2026-10-13","worklist":"interpro-pfam-duf-2026-10-10"},"members":[],"metadata":{"curation_status":"SEEDED","local_source":"source/data/families/PF06452.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":3453,"domain_architectures":503,"matches":6400,"proteins":6161,"proteomes":3332,"structures":7,"taxa":5255},"curation_status":"SEEDED","description":"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. 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