Entry Database : PDB / ID : 5n0f Structure visualization Downloads & linksTitle The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with 1,6-ManSIFG ComponentsAlpha-1,6-mannanase Details Keywords HYDROLASE / glycoside HYDROLASE / complex / mannanase / S-linked polysaccharideFunction / homology Function and homology informationFunction Domain/homology Component
Glycoside hydrolase, family 76 / Glycosyl hydrolase family 76 / Cellulose binding, type IV / Cellulose Binding Domain Type IV / Carbohydrate binding module (family 6) / CBM6 (carbohydrate binding type-6) domain profile. / Carbohydrate binding module family 6 / Glycosyltransferase - #20 / Six-hairpin glycosidase superfamily / Glycosyltransferase ... Glycoside hydrolase, family 76 / Glycosyl hydrolase family 76 / Cellulose binding, type IV / Cellulose Binding Domain Type IV / Carbohydrate binding module (family 6) / CBM6 (carbohydrate binding type-6) domain profile. / Carbohydrate binding module family 6 / Glycosyltransferase - #20 / Six-hairpin glycosidase superfamily / Glycosyltransferase / Alpha/alpha barrel / Galactose-binding-like domain superfamily / Mainly Alpha Similarity search - Domain/homologyBiological species Bacillus circulans (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.69 Å DetailsAuthors Jin, Y. / Williams, S. / Davies, G. Funding support United Kingdom, Australia, 2items Details Hide detailsOrganization Grant number Country European Research Council AdG322942 United Kingdom Australian Research Council FT130100103 Australia
CitationJournal : Chem. Commun. (Camb.) / Year : 2017Title : An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor.Authors : Belz, T. / Jin, Y. / Coines, J. / Rovira, C. / Davies, G.J. / Williams, S.J. History Deposition Feb 2, 2017 Deposition site : PDBE / Processing site : PDBERevision 1.0 Aug 9, 2017 Provider : repository / Type : Initial releaseRevision 1.1 Aug 16, 2017 Group : Database references / Category : citation / citation_authorItem : _citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.titleRevision 1.2 Aug 23, 2017 Group : Database references / Category : citationItem : _citation.journal_volume / _citation.page_first / _citation.page_lastRevision 2.0 Jul 29, 2020 Group : Atomic model / Author supporting evidence ... Atomic model / Author supporting evidence / Derived calculations / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_audit_support / pdbx_entity_nonpoly / struct_site / struct_site_gen Item : _atom_site.auth_atom_id / _atom_site.label_atom_id ... _atom_site.auth_atom_id / _atom_site.label_atom_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_label_atom_id / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_audit_support.funding_organization / _pdbx_entity_nonpoly.name Description : Carbohydrate remediation / Provider : repository / Type : RemediationRevision 2.1 Jan 17, 2024 Group : Data collection / Database references ... Data collection / Database references / Refinement description / Structure summary Category : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item : _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ... _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
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