1XPM

Crystal Structure of Staphylococcus aureus HMG-COA Synthase with HMG-CoA and Acetoacetyl-COA and Acetylated Cysteine

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
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	d1xpma2	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	d1xpma1	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)
A	d1xpma4	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
A	d1xpma3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d1xpmb2	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)
B	d1xpmb1	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)
B	d1xpmb4	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d1xpmb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
C	d1xpmc2	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)
C	d1xpmc1	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)
C	d1xpmc4	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
C	d1xpmc3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
D	d1xpmd2	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)
D	d1xpmd1	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)
D	d1xpmd4	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
D	d1xpmd3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Chalcone synthase-like	8031729	4000864	SCOP2 (2022-06-29)
A	SCOP2 Family	Chalcone synthase-like	8031730	4000864	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thiolase-like	8044107	3000122	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thiolase-like	8044108	3000122	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thiolase-like	8044108	3000122	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thiolase-like	8044108	3000122	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thiolase-like	8044108	3000122	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	HMG_CoA_synt_C	e1xpmA2	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	e1xpmA1	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)
B	HMG_CoA_synt_C	e1xpmB2	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)
B	HMG_CoA_synt_N	e1xpmB1	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)
C	HMG_CoA_synt_C	e1xpmC2	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)
C	HMG_CoA_synt_N	e1xpmC1	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)
D	HMG_CoA_synt_C	e1xpmD2	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)
D	HMG_CoA_synt_N	e1xpmD1	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)
B	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)
C	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (4.3.0)
D	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, B, C, D	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, B, C, D	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, B, C, D	IPR016039	Thiolase-like	Homologous Superfamily
A, B, C, D	IPR013528	Hydroxymethylglutaryl-coenzyme A synthase, N-terminal	Domain
A, B, C, D	IPR011554	Hydroxymethylglutaryl-CoA synthase, prokaryotic	Family
A, B, C, D	IPR013746	Hydroxymethylglutaryl-coenzyme A synthase, C-terminal domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	SCY	Parent Component: CYS RESID: AA0056 PSI-MOD : S-acetyl-L-cysteine MOD:00065

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.