Annotations: 2H5C

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2h5ca_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Prokaryotic proteases	alpha-Lytic protease	(Lysobacter enzymogenes ) [TaxId: 69 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Prokaryotic proteases	8029776	4002151	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Trypsin-like serine proteases	8042155	3000114	SCOP2 (2022-06-29)

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)

Protein Family Annotation Pfam Database Homepage

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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ALPHA-LYTIC PROTEASE	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	proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001254	Serine proteases, trypsin domain	Domain
A	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A	IPR035070	Streptogrisin prodomain	Homologous Superfamily
A	IPR004236	Peptidase S1A, alpha-lytic prodomain	Domain
A	IPR037295	Alpha-lytic protease prodomain	Homologous Superfamily
A	IPR001316	Peptidase S1A, streptogrisin	Family
A	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	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.