1EB6

Deuterolysin from Aspergillus oryzae

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	d1eb6a_	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Fungal zinc peptidase	Fungal zinc peptidase	(Aspergillus oryzae ) [TaxId: 5062 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Fungal zinc peptidase	8023260	4003588	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Metalloproteases (zincins), catalytic domain	8035640	3001975	SCOP2 (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	Aspzincin_M35	e1eb6A1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Aspzincin_M35	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02102	Deuterolysin metalloprotease (M35) family (Peptidase_M35)	Deuterolysin metalloprotease (M35) family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	NEUTRAL PROTEASE II	cation binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase 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	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A	IPR001384	Peptidase M35, deuterolysin	Family
A	IPR050414	Fungal secreted metalloproteinases M35	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	deuterolysin M-CSA #596	Deuterolysin is a zinc metalloproteinase, part of a novel family of zinc metalloproteinases which have an Asp residue as the third zinc binding ligand in addition to the general sequence HEXXH found in all zinc metalloproteinases. It shows a preference for basic protein substrates such as histones, and is of particular importance in the Japanese fermentation industry.	Defined by 5 residues: TYR:A-106HIS:A-128GLU:A-129HIS:A-132ASP:A-143 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.24.39 (PDB Primary Data) Search M-CSA Motif + EC 3.4.24.39

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.