2HIR

SOLUTION STRUCTURE OF RECOMBINANT HIRUDIN AND THE LYS-47 (RIGHT ARROW) GLU MUTANT. A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d2hira_	Small proteins	Knottins (small inhibitors, toxins, lectins)	Leech antihemostatic proteins	Hirudin-like	Hirudin	medicinal leech (Hirudo medicinalis ) [TaxId: 6421 ],	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	Hirudin	e2hirA1	A: few secondary structure elements	X: Leech antihemostatic protein (From Topology)	H: Leech antihemostatic protein (From Topology)	T: Leech antihemostatic protein	F: Hirudin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.70.10.10	Mainly Beta	Distorted Sandwich	Thrombin Inhibitor (Hirudin)	Chain I	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00713	Hirudin (Hirudin)	Hirudin	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	HIRUDIN VARIANT-1	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 negative regulation of proteolysis regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity regulation of primary metabolic process negative regulation of peptidase activity organic substance metabolic process regulation of proteolysis regulation of serine-type peptidase activity proteolysis protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process negative regulation of hydrolase activity negative regulation of proteolysis regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity regulation of primary metabolic process negative regulation of peptidase activity organic substance metabolic process regulation of proteolysis regulation of serine-type peptidase activity proteolysis protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biological process organonitrogen compound metabolic process negative regulation of serine-type peptidase activity 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 macromolecule metabolic process regulation of metabolic process	extracellular region extracellular space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011061	Hirudin/antistatin	Homologous Superfamily
A	IPR000429	Proteinase inhibitor I14, hirudin	Family
A	IPR024793	Thrombin inhibitor hirudin	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.