Annotations: 5HGC

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5hgca1	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	automated matches	Zebra finch (Taeniopygia guttata ) [TaxId: 59729 ],	SCOPe (2.08)
A	d5hgca2	Artifacts	Tags	Tags	Tags	N-terminal Tags	Zebra finch (Taeniopygia guttata ) [TaxId: 59729 ],	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	Serpin	e5hgcA1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
A	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00079	Serpin (serine protease inhibitor) (Serpin)	Serpin (serine protease inhibitor)	Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Serpin	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	negative regulation of hydrolase activity regulation of cellular process negative regulation of proteolysis regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity negative regulation of endopeptidase activity regulation of primary metabolic process negative regulation of peptidase activity regulation of proteolysis proteolysis regulation of endopeptidase activity negative regulation of cellular process protein metabolic process negative regulation of hydrolase activity regulation of cellular process negative regulation of proteolysis regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity negative regulation of endopeptidase activity regulation of primary metabolic process negative regulation of peptidase activity regulation of proteolysis proteolysis regulation of endopeptidase activity negative regulation of cellular process protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biological process regulation of protein metabolic process negative regulation of metabolic process regulation of peptidase activity biological regulation negative regulation of molecular function primary metabolic process regulation of macromolecule metabolic process regulation of molecular function regulation of hydrolase activity metabolic process cellular process macromolecule metabolic process regulation of metabolic process	cellular anatomical structure extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR042178	Serpin superfamily, domain 1	Homologous Superfamily
A	IPR042185	Serpin superfamily, domain 2	Homologous Superfamily
A	IPR036186	Serpin superfamily	Homologous Superfamily
A	IPR000215	Serpin family	Family
A	IPR023796	Serpin domain	Domain

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.