1BAL

THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF (ESCHERICHIA COLI)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1bala_	All alpha proteins	Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex	Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex	Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex	E3-binding domain of dihydrolipoamide succinyltransferase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	E3_binding	e1balA1	A: alpha arrays	X: Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex (From Topology)	H: Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex (From Topology)	T: Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex	F: E3_binding	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	4.10.320.10	Few Secondary Structures	Irregular	Dihydrolipoamide Transferase	E3-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02817	e3 binding domain (E3_binding)	e3 binding domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE	S-succinyltransferase activity catalytic activity, acting on a protein acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity S-acyltransferase activity dihydrolipoyllysine-residue succinyltransferase activity catalytic activity succinyltransferase activity fatty acid binding organic acid binding binding ion binding anion binding S-succinyltransferase activity catalytic activity, acting on a protein acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity S-acyltransferase activity dihydrolipoyllysine-residue succinyltransferase activity catalytic activity succinyltransferase activity fatty acid binding organic acid binding binding ion binding anion binding lipid binding lipoic acid binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds primary metabolic process metabolic process cellular process generation of precursor metabolites and energy lysine metabolic process catabolic process oxoacid metabolic process L-lysine catabolic process aspartate family amino acid metabolic process amino acid metabolic process aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds primary metabolic process metabolic process cellular process generation of precursor metabolites and energy lysine metabolic process catabolic process oxoacid metabolic process L-lysine catabolic process aspartate family amino acid metabolic process amino acid metabolic process acetyl-CoA metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process nucleobase-containing compound metabolic process cellular catabolic process acyl-CoA metabolic process nucleobase-containing small molecule metabolic process carboxylic acid catabolic process L-lysine metabolic process amide catabolic process phosphate-containing compound metabolic process sulfur compound metabolic process small molecule metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process amino acid catabolic process nucleoside phosphate metabolic process aspartate family amino acid catabolic process L-lysine catabolic process to acetyl-CoA via saccharopine lysine catabolic process L-amino acid catabolic process carboxylic acid metabolic process L-amino acid metabolic process purine-containing compound metabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process L-lysine catabolic process to acetyl-CoA organophosphate metabolic process small molecule catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex oxoglutarate dehydrogenase complex catalytic complex oxidoreductase complex tricarboxylic acid cycle heteromeric enzyme complex alpha-ketoacid dehydrogenase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001078	2-oxoacid dehydrogenase acyltransferase, catalytic domain	Domain
A	IPR006255	Dihydrolipoamide succinyltransferase	Family
A	IPR050537	2-oxoacid dehydrogenase	Family
A	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
A	IPR036625	E3-binding domain superfamily	Homologous Superfamily
A	IPR004167	Peripheral subunit-binding domain	Domain
A	IPR011053	Single hybrid motif	Homologous Superfamily
A	IPR003016	2-oxo acid dehydrogenase, lipoyl-binding site	Binding Site
A	IPR000089	Biotin/lipoyl attachment	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.