3HSR | pdb_00003hsr

Crystal structure of Staphylococcus aureus protein SarZ in mixed disulfide form

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d3hsra1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	automated matches	automated matches	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
A	d3hsra2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
B	d3hsrb1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	automated matches	automated matches	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
B	d3hsrb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
C	d3hsrc1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	automated matches	automated matches	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
C	d3hsrc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
D	d3hsrd1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	automated matches	automated matches	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	SCOPe (2.08)
D	d3hsrd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus subsp. aureus str. Newman ) [TaxId: 426430 ],	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	MarR	e3hsrA1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: MarR	ECOD (1.6)
B	MarR	e3hsrB1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: MarR	ECOD (1.6)
C	MarR	e3hsrC1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: MarR	ECOD (1.6)
D	MarR	e3hsrD1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: MarR	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
B	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
C	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
D	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	HTH-type transcriptional regulator sarZ	DNA binding binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity	-	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR000835	MarR-type HTH domain	Domain
A, B, C, D	IPR055166	Transcriptional regulator SarA/SarZ/Rot-like, helix-turn-helix domain	Domain
A, B, C, D	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR036390	Winged helix DNA-binding domain superfamily	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.