Entry Database : PDB / ID : 5b6s Structure visualization Downloads & linksTitle Catalytic domain of Coprinopsis cinerea GH62 alpha-L-arabinofuranosidase ComponentsGlycosyl hydrolase family 62 protein Details Keywords HYDROLASE / Coprinopsis cinerea / alpha-L-arabinofuranosidase / arabinoxylan / GH62 / hemicelluloseFunction / homology Function and homology informationFunction Domain/homology Component
L-arabinose metabolic process / non-reducing end alpha-L-arabinofuranosidase / alpha-L-arabinofuranosidase activity / cellulose binding / xylan catabolic process / extracellular region Similarity search - Function Glycoside hydrolase, family 62, arabinosidase / Glycosyl hydrolase family 62 / CBM1 (carbohydrate binding type-1) domain signature. / Cellulose-binding domain, fungal / Cellulose-binding domain superfamily / Fungal cellulose binding domain / CBM1 (carbohydrate binding type-1) domain profile. / Fungal-type cellulose-binding domain / Glycosyl hydrolase domain; family 43 / 5 Propeller ... Glycoside hydrolase, family 62, arabinosidase / Glycosyl hydrolase family 62 / CBM1 (carbohydrate binding type-1) domain signature. / Cellulose-binding domain, fungal / Cellulose-binding domain superfamily / Fungal cellulose binding domain / CBM1 (carbohydrate binding type-1) domain profile. / Fungal-type cellulose-binding domain / Glycosyl hydrolase domain; family 43 / 5 Propeller / Tachylectin-2; Chain A / Glycosyl hydrolase, five-bladed beta-propellor domain superfamily / Mainly Beta Similarity search - Domain/homologyBiological species Coprinopsis cinerea (fungus)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.7 Å DetailsAuthors Tonozuka, T. Funding support Japan, 1items Details Hide detailsOrganization Grant number Country Japan Society for the Promotion of Science 16K07687 Japan
CitationJournal : Appl. Biochem. Biotechnol. / Year : 2017Title : Structure of the Catalytic Domain of alpha-L-Arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, Provides Insights into Structure-Function Relationships in Glycoside Hydrolase Family 62Authors : Tonozuka, T. / Tanaka, Y. / Okuyama, S. / Miyazaki, T. / Nishikawa, A. / Yoshida, M. History Deposition Jun 1, 2016 Deposition site : PDBJ / Processing site : PDBJRevision 1.0 Sep 7, 2016 Provider : repository / Type : Initial releaseRevision 1.1 Sep 14, 2016 Group : Database referencesRevision 1.2 Feb 15, 2017 Group : Database referencesRevision 1.3 Feb 26, 2020 Group : Data collection / Category : diffrn_source / Item : _diffrn_source.pdbx_synchrotron_siteRevision 1.4 Nov 8, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id
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