Annotations: 1HS6

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1hs6a1	All alpha proteins	alpha-alpha superhelix	ARM repeat	Leukotriene A4 hydrolase C-terminal domain	Leukotriene A4 hydrolase C-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1hs6a2	All beta proteins	Zn aminopeptidase N-terminal domain	Zn aminopeptidase N-terminal domain	Zn aminopeptidase N-terminal domain	Leukotriene A4 hydrolase N-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1hs6a3	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Zn aminopeptidase catalytic domain	Leukotriene A4 hydrolase catalytic domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Leukotriene A4 hydrolase N-terminal domain	8038930	3000390	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Metalloproteases (zincins) catalytic domain	8038934	3001975	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	ARM repeat-like	8038928	3000116	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	PF17900	e1hs6A1	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
A	PF09127	e1hs6A2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF09127	ECOD (1.6)
A	PF01433	e1hs6A3	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
A	3.30.2010.30	Alpha Beta	2-Layer Sandwich	Zincin-like		CATH (4.3.0)
A	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
A	1.25.40.320	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09127	Leukotriene A4 hydrolase, C-terminal (Leuk-A4-hydro_C)	Leukotriene A4 hydrolase, C-terminal	-	Repeat
A	PF01433	Peptidase family M1 domain (Peptidase_M1)	Peptidase family M1 domain	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activ ...	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activity [1].	Domain
A	PF17900	Peptidase M1 N-terminal domain (Peptidase_M1_N)	Peptidase M1 N-terminal domain	This domain is found at the N-terminus of aminopeptidases from the M1 family.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	LEUKOTRIENE A-4 HYDROLASE	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity RNA binding binding organic cyclic compound binding nucleic acid binding metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity metalloexopeptidase activity leukotriene-A4 hydrolase activity peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity RNA binding binding organic cyclic compound binding nucleic acid binding metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity metalloexopeptidase activity leukotriene-A4 hydrolase activity ether hydrolase activity hydrolase activity, acting on ether bonds tripeptidase activity tripeptide aminopeptidase activity epoxide hydrolase activity cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding	icosanoid metabolic process leukotriene metabolic process oxoacid metabolic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process leukotriene biosynthetic process carboxylic acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process icosanoid biosynthetic process organic substance biosynthetic process icosanoid metabolic process leukotriene metabolic process oxoacid metabolic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process leukotriene biosynthetic process carboxylic acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process icosanoid biosynthetic process organic substance biosynthetic process small molecule metabolic process metabolic process cellular process cellular catabolic process catabolic process organic substance catabolic process peptide metabolic process peptide catabolic process response to organic substance response to stimulus response to hormone response to chemical response to endogenous stimulus response to organonitrogen compound response to peptide hormone response to oxygen-containing compound response to nitrogen compound developmental process multicellular organismal process epithelium development cellular developmental process tube development animal organ development respiratory tube development lung epithelium development type I pneumocyte differentiation tissue development epithelial cell differentiation lung epithelial cell differentiation multicellular organism development lung cell differentiation cell differentiation anatomical structure development lung development respiratory system development system development primary metabolic process lipid metabolic process response to metal ion response to zinc ion response to inorganic substance organonitrogen compound metabolic process protein metabolic process macromolecule metabolic process proteolysis	extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol membrane-enclosed lumen extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol membrane-enclosed lumen intracellular vesicle ficolin-1-rich granule intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle organelle lumen cytoplasmic vesicle ficolin-1-rich granule lumen secretory granule secretory vesicle nucleus nucleoplasm nuclear lumen tertiary granule lumen tertiary granule

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR034015	Aminopeptidase, leukotriene A4 hydrolase-like	Family
A	IPR001930	Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase	Family
A	IPR016024	Armadillo-type fold	Homologous Superfamily
A	IPR012777	Leukotriene A4 hydrolase/leucine aminopeptidase	Family
A	IPR042097	Aminopeptidase N-like , N-terminal domain superfamliy	Homologous Superfamily
A	IPR015211	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal	Domain
A	IPR038502	Peptidase M1, LTA-4 hydrolase/aminopeptidase, C-terminal domain superfamily	Homologous Superfamily
A	IPR027268	Peptidase M4/M1, CTD superfamily	Homologous Superfamily
A	IPR014782	Peptidase M1, membrane alanine aminopeptidase	Domain
A	IPR045357	Aminopeptidase N-like , N-terminal domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P09960	atherosclerosis Liver Cirrhosis, Experimental squamous cell carcinoma acute myeloid leukemia cutaneous melanoma hypertensive disorder lung carcinoma ovarian cancer tuberculosis arteriosclerosis disorder depressive disorder lymphoplasmacytic lymphoma non-small cell lung carcinoma small intestine neuroendocrine neoplasm astrocytic tumor atherosclerosis Liver Cirrhosis, Experimental squamous cell carcinoma acute myeloid leukemia cutaneous melanoma hypertensive disorder lung carcinoma ovarian cancer tuberculosis arteriosclerosis disorder depressive disorder lymphoplasmacytic lymphoma non-small cell lung carcinoma small intestine neuroendocrine neoplasm astrocytic tumor malignant mesothelioma osteosarcoma

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

Chains	Enzyme Name	Description	Catalytic Residues
A	leukotriene-A4 hydrolase M-CSA #166	Leukotriene A4 hydrolase/ Aminopeptidase is involved in the immune response in humans, and is unique in its ability to catalyse two very different reactions at the active site. Not only is it able to catalyse the hydrolysis of the epoxide Leukotriene A4 to produce the potent immune activator Leukotriene B4, it is also able to catalyse the hydrolysis of peptide bonds, acting on the first peptide bond after the N terminal. One active site is enough to confer such variety of function, so the enzyme represents a yardstick of evolutionary efficiency seldom reached in nature. It displays a characteristic Zinc binding motif at the active site (GXMEN) which places it in the family M1 of Zinc metalloproteases.	Defined by 7 residues: GLU:A-272 [auth A-271]HIS:A-296 [auth A-295]GLU:A-297 [auth A-296]HIS:A-300 [auth A-299]GLU:A-319 [auth A-318]ASP:A-376 [auth A-375]TYR:A-384 [auth A-383] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.3.2.6 (PDB Primary Data) Search M-CSA Motif + EC 3.3.2.6

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.