1DS2

CRYSTAL STRUCTURE OF SGPB:OMTKY3-COO-LEU18I

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth E]	d1ds2e_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Prokaryotic proteases	Protease B	(Streptomyces griseus ) [TaxId: 1911 ],	SCOPe (2.08)
B [auth I]	d1ds2i_	Small proteins	Kazal-type serine protease inhibitors	Kazal-type serine protease inhibitors	Ovomucoid domain III-like	Ovomucoid domains	turkey (Meleagris gallopavo ) [TaxId: 9103 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth E]	SCOP2B Superfamily	Trypsin-like serine proteases	8035344	3000114	SCOP2B (2022-06-29)
B [auth I]	SCOP2B Superfamily	Kazal-type serine protease inhibitors	8040162	3000605	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 [auth E]	PF00089	e1ds2E1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: PF00089	ECOD (1.6)
B [auth I]	PF00050	e1ds2I1	A: few secondary structure elements	X: Kazal-type serine protease inhibitors-like	H: Kazal-type serine protease inhibitors (From Topology)	T: Kazal-type serine protease inhibitors	F: PF00050	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth E]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B [auth I]	3.30.60.30	Alpha Beta	2-Layer Sandwich	Wheat Germ Agglutinin (Isolectin 2)	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth E]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
B [auth I]	PF00050	Kazal-type serine protease inhibitor domain (Kazal_1)	Kazal-type serine protease inhibitor domain	Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containi ...	Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family Swiss:P46721.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth E]	PROTEINASE B (SGPB)	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	extracellular region cellular anatomical entity
B [auth I]	OVOMUCOID	enzyme regulator activity molecular function inhibitor activity peptidase regulator activity serine-type endopeptidase inhibitor activity molecular function regulator activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E]	IPR001254	Serine proteases, trypsin domain	Domain
A [auth E]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A [auth E]	IPR004236	Peptidase S1A, alpha-lytic prodomain	Domain
A [auth E]	IPR001316	Peptidase S1A, streptogrisin	Family
A [auth E]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A [auth E]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A [auth E]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B [auth I]	IPR036058	Kazal domain superfamily	Homologous Superfamily
B [auth I]	IPR002350	Kazal domain	Domain
B [auth I]	IPR001239	Proteinase inhibitor I1, Kazal-type, metazoa	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A [auth E]	streptogrisin B M-CSA #608	Serine protease B extracted from Streptomyces griseus shows similar active site architecture to the well characterised family of human serine proteases and displays trypsin like specificity for its peptide substrates. It has proved especially useful in analysing the effect of peptide inhibitors such as turkey ovomucoid inhibitor.	Defined by 5 residues: HIS:A-33 [auth E-57]ASP:A-63 [auth E-102]GLY:A-139 [auth E-193]SER:A-141 [auth E-195]SER:A-156 [auth E-214] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.21.81 (PDB Primary Data) Search M-CSA Motif + EC 3.4.21.81

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 R01GM133198.