Entry Database : PDB / ID : 6u3j Structure visualization Downloads & linksTitle Structure of the 2-oxoadipate dehydrogenase DHTKD1 Components2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial Details Keywords OXIDOREDUCTASE / lysine metabolism mitochondrial dehydrogenaseFunction / homology Function and homology informationFunction Domain/homology Component
Oxidoreductases; Acting on the aldehyde or oxo group of donors; With a disulfide as acceptor / oxoglutarate dehydrogenase (succinyl-transferring) activity / oxoglutarate dehydrogenase complex / Glyoxylate metabolism and glycine degradation / thiamine pyrophosphate binding / hematopoietic progenitor cell differentiation / tricarboxylic acid cycle / generation of precursor metabolites and energy / glycolytic process / mitochondrial matrix ... Oxidoreductases; Acting on the aldehyde or oxo group of donors; With a disulfide as acceptor / oxoglutarate dehydrogenase (succinyl-transferring) activity / oxoglutarate dehydrogenase complex / Glyoxylate metabolism and glycine degradation / thiamine pyrophosphate binding / hematopoietic progenitor cell differentiation / tricarboxylic acid cycle / generation of precursor metabolites and energy / glycolytic process / mitochondrial matrix / mitochondrion / cytosol Similarity search - Function Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal / Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain superfamily / 2-oxoglutarate dehydrogenase C-terminal / 2-oxoglutarate dehydrogenase E1 component / Dehydrogenase, E1 component / Dehydrogenase E1 component / Transketolase-like, pyrimidine-binding domain / Transketolase, pyrimidine binding domain / Transketolase, pyrimidine binding domain / Thiamin diphosphate-binding fold Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution : 2.25 Å DetailsAuthors Khamrui, S. / Lazarus, M.B. Funding support United States, 1items Details Hide detailsOrganization Grant number Country National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) GM124838 United States
CitationJournal : Acs Chem.Biol. / Year : 2020Title : Inhibition and Crystal Structure of the Human DHTKD1-Thiamin Diphosphate Complex.Authors: Leandro, J. / Khamrui, S. / Wang, H. / Suebsuwong, C. / Nemeria, N.S. / Huynh, K. / Moustakim, M. / Secor, C. / Wang, M. / Dodatko, T. / Stauffer, B. / Wilson, C.G. / Yu, C. / Arkin, M.R. / ... Authors : Leandro, J. / Khamrui, S. / Wang, H. / Suebsuwong, C. / Nemeria, N.S. / Huynh, K. / Moustakim, M. / Secor, C. / Wang, M. / Dodatko, T. / Stauffer, B. / Wilson, C.G. / Yu, C. / Arkin, M.R. / Jordan, F. / Sanchez, R. / DeVita, R.J. / Lazarus, M.B. / Houten, S.M. History Deposition Aug 21, 2019 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jul 22, 2020 Provider : repository / Type : Initial releaseRevision 1.1 Jul 29, 2020 Group : Database references / Derived calculationsCategory : citation / citation_author ... citation / citation_author / pdbx_struct_conn_angle / struct_conn Item : _citation.country / _citation.journal_abbrev ... _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _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_asym_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 Revision 1.2 Sep 2, 2020 Group : Database references / Category : citation / citation_authorItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID Revision 1.3 Oct 11, 2023 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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