7VEY | pdb_00007vey

Crystal structure of Cyclosorus parasiticus chalcone synthase 1 (CpCHS1)

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ACP_syn_III_C	e7veyA2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
A	Chal_sti_synt_N	e7veyA1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Chal_sti_synt_N	ECOD (1.6)
B	ACP_syn_III_C	e7veyB2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
B	Chal_sti_synt_N	e7veyB1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Chal_sti_synt_N	ECOD (1.6)
C	ACP_syn_III_C	e7veyC2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
C	Chal_sti_synt_N	e7veyC1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Chal_sti_synt_N	ECOD (1.6)
D	ACP_syn_III_C	e7veyD2	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: ACP_syn_III_C	ECOD (1.6)
D	Chal_sti_synt_N	e7veyD1	A: a/b three-layered sandwiches	X: Thiolase-like (From Topology)	H: Thiolase-like (From Topology)	T: Thiolase-like	F: Chal_sti_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 (utative)
B	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (utative)
C	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (utative)
D	3.40.47.10	Alpha Beta	3-Layer(aba) Sandwich	Peroxisomal Thiolase	Chain A, domain 1	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00195	Chalcone and stilbene synthases, N-terminal domain (Chal_sti_synt_N)	Chalcone and stilbene synthases, N-terminal domain	The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.	Domain
A, B, C, D	PF02797	Chalcone and stilbene synthases, C-terminal domain (Chal_sti_synt_C)	Chalcone and stilbene synthases, C-terminal domain	This domain of chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in the N-terminal domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	chalcone synthases	acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	polyketide biosynthetic process secondary metabolite biosynthetic process biosynthetic process polyketide metabolic process metabolic process cellular process secondary metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001099	Chalcone/stilbene synthase, N-terminal	Domain
A, B, C, D	IPR016039	Thiolase-like	Homologous Superfamily
A, B, C, D	IPR012328	Chalcone/stilbene synthase, C-terminal	Domain
A, B, C, D	IPR011141	Polyketide synthase, type III	Family
A, B, C, D	IPR018088	Chalcone/stilbene synthase, active site	Active Site

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.