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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1hfsa_ Alpha and beta proteins (a+b) Zincin-like Metalloproteases ('zincins'), catalytic domain Matrix metalloproteases, catalytic domain Stromelysin-1 (MMP-3) human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyMetalloproteases (zincins), catalytic domain 8035528 3001975 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APeptidase_M10e1hfsA1 A: mixed a+b and a/bX: Zincin-likeH: Metalloproteases (zincins) catalytic domain (From Topology)T: Metalloproteases (zincins) catalytic domainF: Peptidase_M10ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.390.10 Alpha Beta 3-Layer(aba) Sandwich Collagenase (Catalytic Domain) Collagenase (Catalytic Domain)CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00413Matrixin (Peptidase_M10)MatrixinThe members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
STROMELYSIN-1

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

ChainsEnzyme NameDescriptionCatalytic Residues
stromelysin 1  M-CSA #591

Human stromelysin-1 (matrix metalloproteinase 3, MMP-3) is one of the most attractive targets in drug discovery today because of its broad physiological specificity.This extracellular endopeptidase of vertebrate tissues degrades various proteoglycan components of the extracellular matrix as well as fibronectin and laminin. Stromelysin also plays a unique role among the MMPs because of its involvement in activation of other MMP proenzymes.

Defined by 4 residues: HIS:A-114 [auth A-201]GLU:A-115 [auth A-202]HIS:A-118 [auth A-205]HIS:A-124 [auth A-211]
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