6EZ3

Structure of CDPS from Staphylococcus haemolyticus

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Cyclodipeptide synthase-like	8084023	4004834	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotidylyl transferase	8084024	3001541	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Nucleotidylyl transferase	8084024	3001541	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Nucleotidylyl transferase	8084024	3001541	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Nucleotidylyl transferase	8084024	3001541	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Nucleotidylyl transferase	8084024	3001541	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Nucleotidylyl transferase	8084024	3001541	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	PF16715	e6ez3A1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF16715	ECOD (1.6)
B	PF16715	e6ez3B1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF16715	ECOD (1.6)
C	PF16715	e6ez3C1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF16715	ECOD (1.6)
D	PF16715	e6ez3D1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF16715	ECOD (1.6)
E	PF16715	e6ez3E1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF16715	ECOD (1.6)
F	PF16715	e6ez3F1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF16715	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.11710	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Cyclodipeptide synthase	CATH (4.3.0)
B	3.40.50.11710	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Cyclodipeptide synthase	CATH (4.3.0)
C	3.40.50.11710	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Cyclodipeptide synthase	CATH (4.3.0)
D	3.40.50.11710	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Cyclodipeptide synthase	CATH (4.3.0)
E	3.40.50.11710	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Cyclodipeptide synthase	CATH (4.3.0)
F	3.40.50.11710	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Cyclodipeptide synthase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF16715	Cyclodipeptide synthase (CDPS)	Cyclodipeptide synthase	This family of proteins includes enzymes involved in the synthesis of cyclodipeptides using aminoacyl-tRNAs as substrates, including cyclo(L-leucyl-L-leucyl) synthase, cyclo(L-tyrosyl-L-tyrosyl) synthase and cyclo(L-leucyl-L-phenylalanyl) synthase. T ...	This family of proteins includes enzymes involved in the synthesis of cyclodipeptides using aminoacyl-tRNAs as substrates, including cyclo(L-leucyl-L-leucyl) synthase, cyclo(L-tyrosyl-L-tyrosyl) synthase and cyclo(L-leucyl-L-phenylalanyl) synthase. They are structurally similar to class Ic aminoacyl-tRNA synthetases (aaRSs) [1-3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Cyclo(L-leucyl-L-leucyl) synthase	aminoacyltransferase activity acyltransferase activity transferase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR038622	Cyclodipeptide synthase superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR030903	Cyclodipeptide synthase	Family

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 R01GM133198.