3TEX

Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) to 1.7-A resolution

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3texa2	All beta proteins	Anthrax protective antigen N-terminal-like	PA14-like	PA14	PA14	anthrax,anthrax bacterium (Bacillus anthracis ) [TaxId: 1392 ],	SCOPe (2.08)
A	d3texa1	Membrane and cell surface proteins and peptides	Anthrax protective antigen C-terminal-like	Anthrax protective antigen C-terminal-like	Anthrax protective antigen C-terminal-like	Anthrax protective antigen C-terminal-like	anthrax,anthrax bacterium (Bacillus anthracis ) [TaxId: 1392 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Anthrax PA domain 3-like	8054212	3000301	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	FIP-like	8054214	3002056	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GLEYA/PA14-like	8054210	3002282	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GLEYA/PA14-like	8037960	3002282	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	PA14	e3texA17	A: beta sandwiches	X: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	H: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	T: N-terminal beta-sandwich domain in anthrax protective antigen	F: PA14	ECOD (1.6)
A	Binary_toxB_2	e3texA16	A: beta sandwiches	X: Middle beta-sandwich domain in anthrax protective antigen (From Topology)	H: Middle beta-sandwich domain in anthrax protective antigen (From Topology)	T: Middle beta-sandwich domain in anthrax protective antigen	F: Binary_toxB_2	ECOD (1.6)
A	EUF07840	e3texA18	A: beta sandwiches	X: Ig-like domain in anthrax protective antigen (From Topology)	H: Ig-like domain in anthrax protective antigen (From Topology)	T: Ig-like domain in anthrax protective antigen	F: EUF07840	ECOD (1.6)
A	Binary_toxB_3	e3texA19	A: a+b two layers	X: beta-grasp domain in anthrax protective antigen (From Topology)	H: beta-grasp domain in anthrax protective antigen (From Topology)	T: beta-grasp domain in anthrax protective antigen	F: Binary_toxB_3	ECOD (1.6)
A	Binary_toxB	e3texA20	A: few secondary structure elements	X: Ca-binding domain in anthrax protective antigen (From Topology)	H: Ca-binding domain in anthrax protective antigen (From Topology)	T: Ca-binding domain in anthrax protective antigen	F: Binary_toxB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.182.10	Alpha Beta	Alpha-Beta Complex	Toxin - Anthrax Protective Antigen	domain 1	CATH (4.3.0)
A	2.60.120.240	Mainly Beta	Sandwich	Jelly Rolls	Protective antigen, heptamerisation domain	CATH (4.3.0)
A	3.10.20.110	Alpha Beta	Roll	Ubiquitin-like (UB roll)		CATH (4.3.0)
A	2.60.40.810	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF07691	PA14 domain (PA14)	PA14 domain	This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dic ...	This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.	Domain
A	PF17475	Clostridial binary toxin B/anthrax toxin PA domain 2 (Binary_toxB_2)	Clostridial binary toxin B/anthrax toxin PA domain 2	This domain forms the middle beta sandwish domain in anthrax toxin.	Domain
A	PF03495	Clostridial binary toxin B/anthrax toxin PA Ca-binding domain (Binary_toxB)	Clostridial binary toxin B/anthrax toxin PA Ca-binding domain	This domain is a calcium binding domain in the anthrax toxin protective antigen.	Domain
A	PF17476	Clostridial binary toxin B/anthrax toxin PA domain 3 (Binary_toxB_3)	Clostridial binary toxin B/anthrax toxin PA domain 3	This entry represents the beta-grasp domain in anthrax protective antigen.	Domain
A	PF20835	Anthrax protective antigen, immunoglobulin-like domain (PA_Ig-like)	Anthrax protective antigen, immunoglobulin-like domain	Anthrax protective antigen (PA) is one of the three proteins forming the anthrax toxin. It is involved in the first step of toxin entry into host cells, enabling lethal factor (LF) and oedema factor (EF) to cross to the cytosol. PA undergoes cleavage ...	Anthrax protective antigen (PA) is one of the three proteins forming the anthrax toxin. It is involved in the first step of toxin entry into host cells, enabling lethal factor (LF) and oedema factor (EF) to cross to the cytosol. PA undergoes cleavage by Furin to generate PA20 and PA63. The latter, which adopts a ring-shaped heptameric assembly, shows four distinct domains. The fourth domain, a carboxy- terminal receptor-binding domain, shows an initial hairpin and helix, followed by a beta-sandwich with an immunoglobulin-like fold (this entry) [1-5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Protective antigen	toxin activity cation binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding	cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of intracellular signal transduction negative regulation of biological process regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication regulation of intracellular signal transduction intracellular signaling cassette negative regulation of cellular process cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of intracellular signal transduction negative regulation of biological process regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication regulation of intracellular signal transduction intracellular signaling cassette negative regulation of cellular process signal transduction regulation of biological process regulation of signaling negative regulation of response to stimulus biological regulation regulation of MAPK cascade negative regulation of signal transduction regulation of response to stimulus MAPK cascade regulation of cell communication cellular process negative regulation of MAPK cascade positive regulation of apoptotic process in another organism modulation of apoptotic process in another organism biological process involved in interspecies interaction between organisms positive regulation of biological process regulation of programmed cell death regulation of killing of cells of another organism disruption of cell in another organism modulation of process of another organism positive regulation of cellular process killing of cells of another organism positive regulation of programmed cell death regulation of apoptotic process cell death positive regulation of apoptotic process regulation of cell killing apoptotic process disruption of anatomical structure in another organism programmed cell death cell killing cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis	cellular anatomical structure membrane extracellular region host intracellular membrane-bounded organelle host cellular component host intracellular part host cell membrane host cell cytoplasm part host intracellular organelle host cell endosome membrane host cell cytoplasm host cell part host cell endosome host intracellular region cellular anatomical structure membrane extracellular region host intracellular membrane-bounded organelle host cellular component host intracellular part host cell membrane host cell cytoplasm part host intracellular organelle host cell endosome membrane host cell cytoplasm host cell part host cell endosome host intracellular region host cell plasma membrane host cell cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR035331	Clostridial binary toxin B/anthrax toxin PA, domain 3	Domain
A	IPR048853	Anthrax protective antigen, immunoglobulin-like domain	Domain
A	IPR011658	PA14 domain	Domain
A	IPR027439	Protective antigen, heptamerisation domain	Domain
A	IPR035088	Protective antigen, Ca-binding domain	Domain
A	IPR037524	PA14/GLEYA domain	Domain
A	IPR037149	Protective antigen, heptamerisation domain superfamily	Homologous Superfamily
A	IPR003896	Bacterial exotoxin B	Family
A	IPR027441	Protective antigen, domain 4	Homologous Superfamily

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.