4J41

The crystal structure of a secreted protein EsxB (Mutant P67A) from Bacillus anthracis str. Sterne

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family 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	d4j41a1	All alpha proteins	Ferritin-like	EsxAB dimer-like	automated matches	automated matches	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)
A	d4j41a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)
B	d4j41b_	All alpha proteins	Ferritin-like	EsxAB dimer-like	automated matches	automated matches	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)
D	d4j41d_	All alpha proteins	Ferritin-like	EsxAB dimer-like	automated matches	automated matches	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)
E	d4j41e_	All alpha proteins	Ferritin-like	EsxAB dimer-like	automated matches	automated matches	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)
F	d4j41f_	All alpha proteins	Ferritin-like	EsxAB dimer-like	automated matches	automated matches	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)
C	d4j41c_	All alpha proteins	Ferritin-like	EsxAB dimer-like	automated matches	automated matches	anthrax,anthrax bacterium (Bacillus anthracis str. Sterne ) [TaxId: 260799 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	WXG100_1st	e4j41A1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: ESAT-6 like (From Topology)	T: ESAT-6 like	F: WXG100_1st	ECOD (1.6)
B	WXG100_1st	e4j41B2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: ESAT-6 like (From Topology)	T: ESAT-6 like	F: WXG100_1st	ECOD (1.6)
D	WXG100_1st	e4j41D2	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: ESAT-6 like (From Topology)	T: ESAT-6 like	F: WXG100_1st	ECOD (1.6)
E	WXG100_1st	e4j41E3	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: ESAT-6 like (From Topology)	T: ESAT-6 like	F: WXG100_1st	ECOD (1.6)
F	WXG100_1st	e4j41F3	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: ESAT-6 like (From Topology)	T: ESAT-6 like	F: WXG100_1st	ECOD (1.6)
C	WXG100_1st	e4j41C3	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: ESAT-6 like (From Topology)	T: ESAT-6 like	F: WXG100_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	CATH (4.3.0)
B	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	CATH (4.3.0)
D	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	CATH (4.3.0)
E	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	CATH (4.3.0)
F	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	CATH (4.3.0)
C	1.10.287.850	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	HP0062-like domain	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	PF06013	Proteins of 100 residues with WXG (WXG100)	Proteins of 100 residues with WXG	-	Family

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR010310	Type VII secretion system ESAT-6-like	Family
A, B, C, D, E A, B, C, D, E, F	IPR029013	HP0062-like domain superfamily	Homologous Superfamily

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.