4TSQ

Crystal structure of FraC with DHPC bound (crystal form III)

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
Membrane Protein Annotation: OPM
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cytolysin/lectin	8073477	3000379	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cytolysin/lectin	8073477	3000379	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cytolysin/lectin	8073477	3000379	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Cytolysin/lectin	8073477	3000379	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Cytolysin/lectin	8073477	3000379	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Cytolysin/lectin	8073477	3000379	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	Anemone_cytotox	e4tsqA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Osmotin-like (From Topology)	T: Osmotin-like	F: Anemone_cytotox	ECOD (1.6)
B	Anemone_cytotox	e4tsqB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Osmotin-like (From Topology)	T: Osmotin-like	F: Anemone_cytotox	ECOD (1.6)
C	Anemone_cytotox	e4tsqC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Osmotin-like (From Topology)	T: Osmotin-like	F: Anemone_cytotox	ECOD (1.6)
D	Anemone_cytotox	e4tsqD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Osmotin-like (From Topology)	T: Osmotin-like	F: Anemone_cytotox	ECOD (1.6)
E	Anemone_cytotox	e4tsqE1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Osmotin-like (From Topology)	T: Osmotin-like	F: Anemone_cytotox	ECOD (1.6)
F	Anemone_cytotox	e4tsqF1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Osmotin-like (From Topology)	T: Osmotin-like	F: Anemone_cytotox	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.270.20	Mainly Beta	Sandwich	Mutm (Fpg) Protein	Chain: A, domain 2	CATH (4.3.0)
B	2.60.270.20	Mainly Beta	Sandwich	Mutm (Fpg) Protein	Chain: A, domain 2	CATH (4.3.0)
C	2.60.270.20	Mainly Beta	Sandwich	Mutm (Fpg) Protein	Chain: A, domain 2	CATH (4.3.0)
D	2.60.270.20	Mainly Beta	Sandwich	Mutm (Fpg) Protein	Chain: A, domain 2	CATH (4.3.0)
E	2.60.270.20	Mainly Beta	Sandwich	Mutm (Fpg) Protein	Chain: A, domain 2	CATH (4.3.0)
F	2.60.270.20	Mainly Beta	Sandwich	Mutm (Fpg) Protein	Chain: A, domain 2	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	PF06369	Sea anemone cytotoxic protein (Anemone_cytotox)	Sea anemone cytotoxic protein	-	Family

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	Fragaceatoxin C	binding lipid binding toxin activity passive transmembrane transporter activity channel activity transporter activity transmembrane transporter activity identical protein binding protein binding	biological process involved in interspecies interaction between organisms cytolysis in another organism cellular process disruption of cell in another organism disruption of anatomical structure in another organism cytolysis killing of cells of another organism cell killing localization transport monoatomic ion transport monoatomic cation transport establishment of localization cellular component organization biological process involved in interspecies interaction between organisms cytolysis in another organism cellular process disruption of cell in another organism disruption of anatomical structure in another organism cytolysis killing of cells of another organism cell killing localization transport monoatomic ion transport monoatomic cation transport establishment of localization cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular component organization or biogenesis pore complex assembly	cellular anatomical structure extracellular region cell periphery intracellular organelle cell cortex intracellular anatomical structure organelle membraneless organelle nematocyst intracellular membraneless organelle cytoplasm other organism cell membrane other organism part protein-containing complex cellular anatomical structure extracellular region cell periphery intracellular organelle cell cortex intracellular anatomical structure organelle membraneless organelle nematocyst intracellular membraneless organelle cytoplasm other organism cell membrane other organism part protein-containing complex membrane pore complex membrane protein complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR015926	Cytolysin/lectin	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR050677	Actinoporin Pore-Forming Toxin	Family
A, B, C, D, E A, B, C, D, E, F	IPR009104	Sea anemone actinoporin-like	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D, E A, B, C, D, E, F	OPM	Monotopic/peripheral	All beta monotopic/peripheral	Membrane attack complex superfamily	Anemone pore-forming cytolysin

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C, D, E A, B, C, D, E, F	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	Adventitious Membrane Proteins: Alpha-helical Pore-forming Toxins.	FraC toxin pore with bound lipids

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.