1SOZ

Crystal Structure of DegS protease in complex with an activating peptide

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	d1soza1	All beta proteins	PDZ domain-like	PDZ domain-like	HtrA-like serine proteases	Stress sensor protease DegS, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1soza2	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Prokaryotic proteases	Stress sensor protease DegS, catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1soza3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1sozb1	All beta proteins	PDZ domain-like	PDZ domain-like	HtrA-like serine proteases	Stress sensor protease DegS, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1sozb2	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Prokaryotic proteases	Stress sensor protease DegS, catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1sozb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1sozc1	All beta proteins	PDZ domain-like	PDZ domain-like	HtrA-like serine proteases	Stress sensor protease DegS, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1sozc2	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Prokaryotic proteases	Stress sensor protease DegS, catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1sozc3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Trypsin-like serine proteases	8042458	3000114	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Trypsin-like serine proteases	8042458	3000114	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Trypsin-like serine proteases	8042458	3000114	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	PF13365	e1sozA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel	F: PF13365	ECOD (1.6)
A	PF00595	e1sozA2	A: beta barrels	X: PDZ domain (From Topology)	H: PDZ domain (From Topology)	T: PDZ domain	F: PF00595	ECOD (1.6)
B	PF13365	e1sozB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: PF13365	ECOD (1.6)
B	PF13180	e1sozB2	A: beta barrels	X: PDZ domain (From Topology)	H: PDZ domain (From Topology)	T: PDZ domain	F: PF13180	ECOD (1.6)
C	PF13365	e1sozC2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: PF13365	ECOD (1.6)
C	PF13180	e1sozC1	A: beta barrels	X: PDZ domain (From Topology)	H: PDZ domain (From Topology)	T: PDZ domain	F: PF13180	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
A	2.30.42.10	Mainly Beta	Roll	Pdz3 Domain	PDZ domain	CATH (4.3.0)
B	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B	2.30.42.10	Mainly Beta	Roll	Pdz3 Domain	PDZ domain	CATH (4.3.0)
C	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Protease degS	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity identical protein binding protein binding binding	cellular response to stimulus response to organic substance cellular response to topologically incorrect protein response to stimulus cellular response to misfolded protein cellular response to chemical stimulus response to misfolded protein cellular response to stress response to chemical response to stress response to topologically incorrect protein cellular process cellular response to organic substance organic substance metabolic process cellular response to stimulus response to organic substance cellular response to topologically incorrect protein response to stimulus cellular response to misfolded protein cellular response to chemical stimulus response to misfolded protein cellular response to stress response to chemical response to stress response to topologically incorrect protein cellular process cellular response to organic substance organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery plasma membrane membrane cellular anatomical entity outer membrane-bounded periplasmic space cell envelope periplasmic space
D, E	activating peptide	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A, B, C	IPR001940	Peptidase S1C	Family
A, B, C	IPR036034	PDZ superfamily	Homologous Superfamily
A, B, C	IPR011783	Peptidase S1C, DegS	Family
A, B, C	IPR001478	PDZ domain	Domain
A, B, C	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	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.