Entry Database : PDB / ID : 5csl Structure visualization Downloads & linksTitle Crystal structure of the 500 kD yeast acetyl-CoA carboxylase holoenzyme dimer ComponentsAcetyl-CoA carboxylase Details Keywords LIGASE / acetyl-CoA carboxylaseFunction / homology Function and homology informationFunction Domain/homology Component
: / Biotin transport and metabolism / Fatty acyl-CoA biosynthesis / Carnitine metabolism / acetyl-CoA carboxylase / carboxyl- or carbamoyltransferase activity / acetyl-CoA binding / biotin carboxylase / acetyl-CoA carboxylase complex / biotin carboxylase activity ... : / Biotin transport and metabolism / Fatty acyl-CoA biosynthesis / Carnitine metabolism / acetyl-CoA carboxylase / carboxyl- or carbamoyltransferase activity / acetyl-CoA binding / biotin carboxylase / acetyl-CoA carboxylase complex / biotin carboxylase activity / malonyl-CoA biosynthetic process / acetyl-CoA carboxylase activity / acetyl-CoA biosynthetic process / long-chain fatty acid biosynthetic process / fatty acid biosynthetic process / protein import into nucleus / endoplasmic reticulum membrane / protein homodimerization activity / mitochondrion / ATP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function Acetyl-CoA carboxylase, central domain / : / : / Acetyl-CoA carboxylase, central region / Acetyl-CoA carboxylase, BT domain / Acetyl-coenzyme A carboxyltransferase, C-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile. / Acetyl-coenzyme A carboxyltransferase, N-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile. / Acetyl-CoA carboxylase ... Acetyl-CoA carboxylase, central domain / : / : / Acetyl-CoA carboxylase, central region / Acetyl-CoA carboxylase, BT domain / Acetyl-coenzyme A carboxyltransferase, C-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile. / Acetyl-coenzyme A carboxyltransferase, N-terminal / Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile. / Acetyl-CoA carboxylase / Carboxyl transferase domain / Biotin-binding site / Biotin-requiring enzymes attachment site. / Biotin carboxylase-like, N-terminal domain / Biotin carboxylase, C-terminal / Biotin carboxylation domain / Biotin carboxylase, N-terminal domain / Biotin carboxylase C-terminal domain / Biotin carboxylation domain profile. / Biotin carboxylase C-terminal domain / Carbamoyl-phosphate synthase subdomain signature 1. / Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain / Carbamoyl-phosphate synthase L chain, ATP binding domain / Biotin-requiring enzyme / Rudiment single hybrid motif / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / ATP-grasp fold, subdomain 1 / Pre-ATP-grasp domain superfamily / ATP-grasp fold / ATP-grasp fold profile. / ClpP/crotonase-like domain superfamily / Carbamoyl-phosphate synthase subdomain signature 2. Similarity search - Domain/homologyBiological species Saccharomyces cerevisiae (brewer's yeast)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution : 3.2 Å DetailsAuthors Wei, J. / Tong, L. Funding support United States, 2items Details Hide detailsOrganization Grant number Country National Institutes of Health/Office of the Director OD012018 United States National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK) DK067238 United States
CitationJournal : Nature / Year : 2015Title : Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer.Authors : Wei, J. / Tong, L. History Deposition Jul 23, 2015 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Oct 28, 2015 Provider : repository / Type : Initial releaseRevision 1.1 Nov 11, 2015 Group : Database referencesRevision 1.2 Sep 20, 2017 Group : Author supporting evidence / Derived calculations / Category : pdbx_audit_support / pdbx_struct_oper_listItem : _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operationRevision 1.3 Mar 23, 2022 Group : Author supporting evidence / Database references / Category : database_2 / pdbx_audit_supportItem : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organization / _pdbx_audit_support.grant_number
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