1CTS

CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF TWO DIFFERENT FORMS OF CITRATE SYNTHASE AT 2.7 AND 1.7 ANGSTROMS RESOLUTION

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d1ctsa_	All alpha proteins	Citrate synthase	Citrate synthase	Citrate synthase	Citrate synthase	pig (Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Citrate synthase	8038438	3001050	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Citrate_synt	e1ctsA1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.580.10	Mainly Alpha	Orthogonal Bundle	Citrate Synthase	domain 1	CATH (4.3.0)
A	1.10.230.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450-Terp	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00285	Citrate synthase, C-terminal domain (Citrate_synt)	Citrate synthase, C-terminal domain	This is the long, C-terminal part of the enzyme.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CITRATE SYNTHASE	citrate synthase activity acyltransferase activity acyltransferase activity, acyl groups converted into alkyl on transfer transferase activity catalytic activity citrate (Si)-synthase activity identical protein binding protein binding binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy carbohydrate metabolic process tricarboxylic acid metabolic process oxoacid metabolic process carboxylic acid metabolic process small molecule metabolic process organic acid metabolic process aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy carbohydrate metabolic process tricarboxylic acid metabolic process oxoacid metabolic process carboxylic acid metabolic process small molecule metabolic process organic acid metabolic process citrate metabolic process	membrane-bounded organelle intracellular anatomical structure mitochondrion membrane-enclosed lumen intracellular membrane-bounded organelle mitochondrial matrix intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR010109	Citrate synthase, eukaryotic-type	Family
A	IPR019810	Citrate synthase active site	Active Site
A	IPR016143	Citrate synthase-like, small alpha subdomain	Homologous Superfamily
A	IPR036969	Citrate synthase superfamily	Homologous Superfamily
A	IPR002020	Citrate synthase	Family
A	IPR016142	Citrate synthase-like, large alpha subdomain	Homologous Superfamily

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.