4ZCS

Crystal structure of the C-terminal catalytic domain of Plasmodium falciparum CTP:phosphocholine cytidylyltransferase in complex with CDP-choline

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth C]	d4zcsc_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
F	d4zcsf_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
A	d4zcsa_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
C [auth E]	d4zcse_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
D [auth B]	d4zcsb_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)
E [auth D]	d4zcsd_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	automated matches	automated matches	(Plasmodium falciparum 3D7 ) [TaxId: 36329 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth C]	CTP_transf_like_1	e4zcsC1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)
F	CTP_transf_like_1	e4zcsF1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)
A	CTP_transf_like_1	e4zcsA1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)
C [auth E]	CTP_transf_like_1	e4zcsE1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)
D [auth B]	CTP_transf_like_1	e4zcsB1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)
E [auth D]	CTP_transf_like_1	e4zcsD1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: CTP_transf_like_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth C]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
F	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
C [auth E]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
D [auth B]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
E [auth D]	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C], C [auth E], D [auth B], E [auth D], A, B [auth C], C [auth E], D [auth B], E [auth D], F	PF01467	Cytidylyltransferase-like (CTP_transf_like)	Cytidylyltransferase-like	This family includes: Cholinephosphate cytidylyltransferase Swiss:P49585; glycerol-3-phosphate cytidylyltransferase Swiss:P27623. It also includes putative adenylyltransferases, and FAD synthases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C], C [auth E], D [auth B], E [auth D], A, B [auth C], C [auth E], D [auth B], E [auth D], F	Choline-phosphate cytidylyltransferase	cytidylyltransferase activity choline-phosphate cytidylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding ion binding binding phosphatidylcholine binding phospholipid binding lipid binding quaternary ammonium group binding small molecule binding cytidylyltransferase activity choline-phosphate cytidylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding ion binding binding phosphatidylcholine binding phospholipid binding lipid binding quaternary ammonium group binding small molecule binding identical protein binding protein binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C], C [auth E], D [auth B], E [auth D], A, B [auth C], C [auth E], D [auth B], E [auth D], F	IPR041723	CTP:phosphocholine cytidylyltransferase domain	Domain
A, B [auth C], C [auth E], D [auth B], E [auth D], A, B [auth C], C [auth E], D [auth B], E [auth D], F	IPR004821	Cytidyltransferase-like domain	Domain
A, B [auth C], C [auth E], D [auth B], E [auth D], A, B [auth C], C [auth E], D [auth B], E [auth D], F	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
A, B [auth C], C [auth E], D [auth B], E [auth D], A, B [auth C], C [auth E], D [auth B], E [auth D], F	IPR045049	Choline-phosphate cytidylyltransferase Pcy1-like	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 R01GM157729.