Entry Database : PDB / ID : 1w8n Structure visualization Downloads & linksTitle Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. ComponentsBACTERIAL SIALIDASE Details Keywords HYDROLASE / GLYCOSIDASE / NEURAMINIDASE / BETA- PROPELLER FOLD.Function / homology Function and homology informationFunction Domain/homology Component
ganglioside catabolic process / oligosaccharide catabolic process / exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / exo-alpha-sialidase / intracellular membrane-bounded organelle / extracellular region / membrane / cytoplasm Similarity search - Function Alpha-galactosidase, NEW3 domain / NPCBM-associated, NEW3 domain of alpha-galactosidase / BNR repeat-like domain / Sialidase family / Sialidase / Coagulation factor 5/8 C-terminal domain, discoidin domain / Coagulation factors 5/8 type C domain (FA58C) profile. / F5/8 type C domain / Coagulation factor 5/8 C-terminal domain / Neuraminidase - #10 ... Alpha-galactosidase, NEW3 domain / NPCBM-associated, NEW3 domain of alpha-galactosidase / BNR repeat-like domain / Sialidase family / Sialidase / Coagulation factor 5/8 C-terminal domain, discoidin domain / Coagulation factors 5/8 type C domain (FA58C) profile. / F5/8 type C domain / Coagulation factor 5/8 C-terminal domain / Neuraminidase - #10 / Sialidase superfamily / Galactose-binding domain-like / 6 Propeller / Neuraminidase / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Galactose-binding-like domain superfamily / Immunoglobulin E-set / Jelly Rolls / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta Similarity search - Domain/homologyBiological species MICROMONOSPORA VIRIDIFACIENS (bacteria)Method X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution : 2.1 Å DetailsAuthors Newstead, S. / Watson, J.N. / Dookhun, V. / Bennet, A.J. / Taylor, G. CitationJournal : FEBS Lett. / Year : 2004Title : Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora ViridifaciensAuthors : Watson, J.N. / Newstead, S. / Dookhun, V. / Taylor, G. / Bennet, A.J. History Deposition Sep 24, 2004 Deposition site : PDBE / Processing site : PDBERevision 1.0 Sep 30, 2004 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Version format complianceRevision 1.2 Jul 5, 2017 Group : Data collection / Category : diffrn_source / Item : _diffrn_source.typeRevision 1.3 Jul 29, 2020 Group : Data collection / Derived calculations ... Data collection / Derived calculations / Other / Structure summary Category : chem_comp / entity ... chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen Item : _chem_comp.name / _chem_comp.type ... _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id Description : Carbohydrate remediation / Provider : repository / Type : RemediationRevision 1.4 Dec 13, 2023 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 Item : _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.