Entry Database : PDB / ID : 2vu0 Structure visualization Downloads & linksTitle Biosynthetic thiolase from Z. ramigera. Complex of the oxidised enzyme with coenzyme A. ComponentsAcetyl-CoA acetyltransferase Details Keywords TRANSFERASE / ACYLTRANSFERASE / PHB BIOSYNTHESISFunction / homology Function and homology informationFunction Domain/homology Component
poly-hydroxybutyrate biosynthetic process / acetyl-CoA C-acetyltransferase / acetyl-CoA C-acetyltransferase activity / cytoplasm Similarity search - Function Thiolase, active site / Thiolases active site. / Thiolase, acyl-enzyme intermediate active site / Thiolases acyl-enzyme intermediate signature. / Thiolase, conserved site / Thiolases signature 2. / Thiolase / Thiolase, C-terminal / Thiolase, C-terminal domain / Thiolase, N-terminal ... Thiolase, active site / Thiolases active site. / Thiolase, acyl-enzyme intermediate active site / Thiolases acyl-enzyme intermediate signature. / Thiolase, conserved site / Thiolases signature 2. / Thiolase / Thiolase, C-terminal / Thiolase, C-terminal domain / Thiolase, N-terminal / Thiolase, N-terminal domain / Thiolase/Chalcone synthase / Peroxisomal Thiolase; Chain A, domain 1 / Thiolase-like / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Zoogloea ramigera (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.87 Å DetailsAuthors Kursula, P. / Wierenga, R.K. CitationJournal : FEBS J. / Year : 2008Title : The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme.Authors : Merilainen, G. / Schmitz, W. / Wierenga, R.K. / Kursula, P. History Deposition May 19, 2008 Deposition site : PDBE / Processing site : PDBERevision 1.0 Oct 28, 2008 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Refinement description / Version format complianceRevision 1.2 Jun 13, 2018 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary Category : citation / diffrn_source ... citation / diffrn_source / entity / entity_name_com / entity_src_gen / pdbx_struct_mod_residue / struct_ref / struct_ref_seq_dif Item : _citation.journal_id_ISSN / _citation.page_last ... _citation.journal_id_ISSN / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _diffrn_source.pdbx_synchrotron_site / _entity.pdbx_description / _entity_name_com.name / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_seq_type / _pdbx_struct_mod_residue.details / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq_dif.align_id / _struct_ref_seq_dif.pdbx_auth_seq_num / _struct_ref_seq_dif.pdbx_pdb_strand_id / _struct_ref_seq_dif.seq_num Revision 1.3 Jul 10, 2019 Group : Data collection / Derived calculations / Category : diffrn_source / struct_connItem : _diffrn_source.pdbx_synchrotron_site / _struct_conn.pdbx_leaving_atom_flagRevision 1.4 Jul 24, 2019 Group : Data collection / Category : diffrn_source / Item : _diffrn_source.pdbx_synchrotron_site
Show all Show less Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.