1TVZ

Crystal structure of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from Staphylococcus aureus

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1tvza2	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Chalcone synthase-like	3-hydroxy-3-methylglutaryl CoA synthase MvaS, C-terminal domain	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
A	d1tvza1	Alpha and beta proteins (a/b)	Thiolase-like	Thiolase-like	Chalcone synthase-like	3-hydroxy-3-methylglutaryl CoA synthase MvaS, N-terminal domain	(Staphylococcus aureus ) [TaxId: 1280 ],	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	HMG_CoA_synt_C	e1tvzA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: HMG_CoA_synt_C	ECOD (1.6)
A	HMG_CoA_synt_N	e1tvzA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: HMG_CoA_synt_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08540	Hydroxymethylglutaryl-coenzyme A synthase C terminal (HMG_CoA_synt_C)	Hydroxymethylglutaryl-coenzyme A synthase C terminal	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	3-hydroxy-3-methylglutaryl-CoA synthase	hydroxymethylglutaryl-CoA synthase activity acyltransferase activity acyltransferase activity, acyl groups converted into alkyl on transfer transferase activity catalytic activity	nucleoside phosphate metabolic process primary metabolic process acetyl-CoA metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process sulfur compound metabolic process small molecule metabolic process amide metabolic process nucleoside phosphate metabolic process primary metabolic process acetyl-CoA metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process sulfur compound metabolic process small molecule metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016039	Thiolase-like	Homologous Superfamily
A	IPR013528	Hydroxymethylglutaryl-coenzyme A synthase, N-terminal	Domain
A	IPR011554	Hydroxymethylglutaryl-CoA synthase, prokaryotic	Family
A	IPR013746	Hydroxymethylglutaryl-coenzyme A synthase, C-terminal domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	CSD	Parent Component: CYS RESID: AA0262 PSI-MOD : L-cysteine sulfinic acid MOD:00267

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.