Entry Database : PDB / ID : 2vfv Structure visualization Downloads & linksTitle Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sulphite ComponentsXYLITOL OXIDASE Details Keywords OXIDOREDUCTASE / FAD / SUGAR / POLYOL / FLAVIN / OXIDASE / FLAVOPROTEINFunction / homology Function and homology informationFunction Domain/homology Component
alditol oxidase / xylitol oxidase activity / L-gulono-1,4-lactone dehydrogenase activity / D-arabinono-1,4-lactone oxidase activity / FAD binding / membrane Similarity search - Function Alpha-Beta Plaits - #2520 / Alpha-Beta Plaits - #2530 / L-gulonolactone/D-arabinono-1,4-lactone oxidase / D-arabinono-1,4-lactone oxidase, C-terminal domain / D-arabinono-1,4-lactone oxidase / Vanillyl-alcohol Oxidase; Chain A, domain 4 / Vanillyl-alcohol Oxidase; Chain A, domain 4 / Vanillyl-alcohol oxidase, C-terminal subdomain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 ... Alpha-Beta Plaits - #2520 / Alpha-Beta Plaits - #2530 / L-gulonolactone/D-arabinono-1,4-lactone oxidase / D-arabinono-1,4-lactone oxidase, C-terminal domain / D-arabinono-1,4-lactone oxidase / Vanillyl-alcohol Oxidase; Chain A, domain 4 / Vanillyl-alcohol Oxidase; Chain A, domain 4 / Vanillyl-alcohol oxidase, C-terminal subdomain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 - #10 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 / FAD linked oxidase, N-terminal / FAD binding domain / FAD-binding, type PCMH, subdomain 1 / FAD-binding domain, PCMH-type / PCMH-type FAD-binding domain profile. / FAD-binding, type PCMH, subdomain 2 / FAD-binding, type PCMH-like superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta Similarity search - Domain/homologyBiological species STREPTOMYCES COELICOLOR (bacteria)Method X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution : 1.72 Å DetailsAuthors Forneris, F. / Mattevi, A. CitationJournal : Biochemistry / Year : 2008Title : Structural Analysis of the Catalytic Mechanism and Stereoselectivity in Streptomyces Coelicolor Alditol Oxidase.Authors : Forneris, F. / Heuts, D.P.H.M. / Delvecchio, M. / Rovida, S. / Fraaije, M.W. / Mattevi, A. History Deposition Nov 5, 2007 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jan 8, 2008 Provider : repository / Type : Initial releaseRevision 1.1 May 8, 2011 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag
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.