1HFS
CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-764,004
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
- Pharos: Disease Associations
- 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 | d1hfsa_ | 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
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Peptidase_M10 | e1hfsA1 | A: mixed a+b and a/b | X: Zincin-like | H: Metalloproteases (zincins) catalytic domain (From Topology) | T: Metalloproteases (zincins) catalytic domain | F: Peptidase_M10 | 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 |
---|---|---|---|---|---|
PF00413 | Matrixin (Peptidase_M10) | Matrixin | The 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
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR018486 | Hemopexin, conserved site | Conserved Site | |
IPR036375 | Hemopexin-like domain superfamily | Homologous Superfamily | |
IPR021158 | Peptidase M10A, cysteine switch, zinc binding site | Binding Site | |
IPR036365 | PGBD-like superfamily | Homologous Superfamily | |
IPR001818 | Peptidase M10, metallopeptidase | Domain | |
IPR021190 | Peptidase M10A | Family | |
IPR002477 | Peptidoglycan binding-like | Domain | |
IPR006026 | Peptidase, metallopeptidase | Domain | |
IPR024079 | Metallopeptidase, catalytic domain superfamily | Homologous Superfamily | |
IPR018487 | Hemopexin-like repeats | Repeat | |
IPR000585 | Hemopexin-like domain | Domain | |
IPR033739 | Peptidase M10A, catalytic domain | Domain |
Pharos: Disease Associations Pharos Homepage Annotation
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic 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] | EC: 3.4.24.17 (PDB Primary Data) |