5IMW

Trapped Toxin

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
Membrane Protein Annotation: mpstruc

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5imwa2	All beta proteins	Perfringolysin C-terminal-like	Perfringolysin C-terminal-like	Perfringolysin C-terminal-like	Intermedilysin C-terminal domain	(Streptococcus intermedius ) [TaxId: 1338 ],	SCOPe (2.08)
A	d5imwa1	Membrane and cell surface proteins and peptides	Perfringolysin N-terminal-like	Perfringolysin N-terminal-like	Perfringolysin N-terminal-like	Intermedilysin N-terminal domain	(Streptococcus intermedius ) [TaxId: 1338 ],	SCOPe (2.08)
B	d5imwb2	All beta proteins	Perfringolysin C-terminal-like	Perfringolysin C-terminal-like	Perfringolysin C-terminal-like	Intermedilysin C-terminal domain	(Streptococcus intermedius ) [TaxId: 1338 ],	SCOPe (2.08)
B	d5imwb1	Membrane and cell surface proteins and peptides	Perfringolysin N-terminal-like	Perfringolysin N-terminal-like	Perfringolysin N-terminal-like	Intermedilysin N-terminal domain	(Streptococcus intermedius ) [TaxId: 1338 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	CDC membrane-sensing domain-like	8052023	3000285	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	MAC/CDC-like	8052024	3002081	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	MAC/CDC-like	8052024	3002081	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CDC membrane-sensing domain-like	8052023	3000285	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	Thiol_cytolys_C	e5imwA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Perfringolysin O beta sandwich domain (From Topology)	T: Perfringolysin O beta sandwich domain	F: Thiol_cytolys_C	ECOD (1.6)
A	Thiol_cytolysin	e5imwA2	A: beta complex topology	X: Membrane attack complex/perforin (MACPF) and cholesterol-dependent cytolysin (CDC) domains (From Topology)	H: Membrane attack complex/perforin (MACPF) and cholesterol-dependent cytolysin (CDC) domains (From Topology)	T: Membrane attack complex/perforin (MACPF) and cholesterol-dependent cytolysin (CDC) domains	F: Thiol_cytolysin	ECOD (1.6)
B	Thiol_cytolys_C	e5imwB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Perfringolysin O beta sandwich domain (From Topology)	T: Perfringolysin O beta sandwich domain	F: Thiol_cytolys_C	ECOD (1.6)
B	Thiol_cytolysin	e5imwB2	A: beta complex topology	X: Membrane attack complex/perforin (MACPF) and cholesterol-dependent cytolysin (CDC) domains (From Topology)	H: Membrane attack complex/perforin (MACPF) and cholesterol-dependent cytolysin (CDC) domains (From Topology)	T: Membrane attack complex/perforin (MACPF) and cholesterol-dependent cytolysin (CDC) domains	F: Thiol_cytolysin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.840.10	Alpha Beta	Alpha-Beta Complex	HIV-1 Reverse Transcriptase	Chain A, domain 3	CATH (utative)
A	3.30.1040.20	Alpha Beta	2-Layer Sandwich	Carboxypeptidase Inhibitor	Chain A	CATH (utative)
A	3.40.30.40	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Perfringolysin	CATH (utative)
A	2.60.40.1430	Mainly Beta	Sandwich	Immunoglobulin-like	Perfringolysin, domain 4	CATH (utative)
B	3.90.840.10	Alpha Beta	Alpha-Beta Complex	HIV-1 Reverse Transcriptase	Chain A, domain 3	CATH (utative)
B	3.30.1040.20	Alpha Beta	2-Layer Sandwich	Carboxypeptidase Inhibitor	Chain A	CATH (utative)
B	3.40.30.40	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Perfringolysin	CATH (utative)
B	2.60.40.1430	Mainly Beta	Sandwich	Immunoglobulin-like	Perfringolysin, domain 4	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF17440	Thiol-activated cytolysin beta sandwich domain (Thiol_cytolys_C)	Thiol-activated cytolysin beta sandwich domain	This domain has an immunoglobulin like fold. It is found at the C-terminus of the thiol-activated cytolsin protein.	Domain
A, B	PF01289	Thiol-activated cytolysin (Thiol_cytolysin)	Thiol-activated cytolysin	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Intermedilysin	sterol binding binding organic cyclic compound binding alcohol binding steroid binding lipid binding cholesterol binding small molecule binding cation binding ion binding metal ion binding toxin activity	biological process involved in interspecies interaction between organisms cellular process disruption of cell in another organism disruption of anatomical structure in another organism killing of cells of another organism cell killing	membrane cellular anatomical entity host cell plasma membrane host cellular component host cell part host cell membrane extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR038700	Thiol-activated cytolysin, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR036359	Thiol-activated cytolysin superfamily	Homologous Superfamily
A, B	IPR035390	Thiol-activated cytolysin C-terminal	Domain
A, B	IPR001869	Thiol-activated cytolysin	Family
A, B	IPR036363	Thiol-activated cytolysin, alpha-beta domain superfamily	Homologous Superfamily

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B	mpstruc	TRANSMEMBRANE PROTEINS: BETA-BARREL	Adventitious Membrane Proteins: Beta-sheet Pore-forming Toxins/Attack Complexes	ILY^ml Cholesterol-dependent cytolysin, CD59-responsive

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.