Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
3.4.24.17
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases;
stromelysin 1
PDB | Resolution (Å) | PDB name |
---|---|---|
1B3D | 2.3 | STROMELYSIN-1 |
1B8Y | 2.0 | X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXED WITH NON-PEPTIDE INHIBITORS: IMPLICATIONS FOR INHIBITOR SELECTIVITY |
1BIW | 2.5 | DESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORS |
1BM6 | SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 COMPLEXED TO A POTENT NON-PEPTIDIC INHIBITOR, NMR, 20 STRUCTURES | |
1BQO | 2.3 | DISCOVERY OF POTENT, ACHIRAL MATRIX METALLOPROTEINASE INHIBITORS |
1C3I | 1.83 | HUMAN STROMELYSIN-1 CATALYTIC DOMAIN COMPLEXED WITH RO-26-2812 |
1C8T | 2.6 | HUMAN STROMELYSIN-1 (E202Q) CATALYTIC DOMAIN COMPLEXED WITH RO-26-2812 |
1CAQ | 1.8 | X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXES WITH NON-PEPTIDE INHIBITORS: IMPLICATION FOR INHIBITOR SELECTIVITY |
1CIZ | 1.64 | X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXES WITH NON-PEPTIDE INHIBITORS: IMPLICATION FOR INHIBITOR SELECTIVITY |
1CQR | 2.0 | CRYSTAL STRUCTURE OF THE STROMELYSIN CATALYTIC DOMAIN AT 2.0 A RESOLUTION |
1D5J | 2.6 | CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A THIAZEPINE BASED INHIBITOR. |
1D7X | 2.0 | CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A MODIFIED PROLINE SCAFFOLD BASED INHIBITOR. |
1D8F | 2.4 | CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A PIPERAZINE BASED INHIBITOR. |
1D8M | 2.44 | CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A HETEROCYCLE-BASED INHIBITOR |
1G05 | 2.45 | HETEROCYCLE-BASED MMP INHIBITOR WITH P2'SUBSTITUENTS |
1G49 | 1.9 | A CARBOXYLIC ACID BASED INHIBITOR IN COMPLEX WITH MMP3 |
1G4K | 2.0 | X-ray Structure of a Novel Matrix Metalloproteinase Inhibitor Complexed to Stromelysin |
1HFS | 1.7 | CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-764,004 |
1HY7 | 1.5 | A CARBOXYLIC ACID BASED INHIBITOR IN COMPLEX WITH MMP3 |
1OO9 | Orientation in Solution of MMP-3 Catalytic Domain and N-TIMP-1 from Residual Dipolar Couplings | |
1QIA | 2.0 | CRYSTAL STRUCTURE OF STROMELYSIN CATALYTIC DOMAIN |
1QIC | 2.0 | CRYSTAL STRUCTURE OF STROMELYSIN CATALYTIC DOMAIN |
1SLM | 1.9 | CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME |
1SLN | 2.27 | CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842 |
1UEA | 2.8 | MMP-3/TIMP-1 COMPLEX |
1UMS | STROMELYSIN-1 CATALYTIC DOMAIN WITH HYDROPHOBIC INHIBITOR BOUND, PH 7.0, 32OC, 20 MM CACL2, 15% ACETONITRILE; NMR ENSEMBLE OF 20 STRUCTURES | |
1UMT | Stromelysin-1 catalytic domain with hydrophobic inhibitor bound, ph 7.0, 32oc, 20 mm cacl2, 15% acetonitrile; nmr average of 20 structures minimized with restraints | |
1USN | 1.8 | CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THIADIAZOLE INHIBITOR PNU-142372 |
2D1O | 2.02 | Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor |
2JNP | Solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH) | |
2JT5 | solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of n-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid (MLC88) | |
2JT6 | Solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of 3-4'-cyanobyphenyl-4-yloxy)-n-hdydroxypropionamide (MMP-3 inhibitor VII) | |
2SRT | CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR | |
2USN | 2.2 | CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THIADIAZOLE INHIBITOR PNU-141803 |
3OHL | 2.36 | catalytic domain of stromelysin-1 in complex with N-Hydroxy-2-(4-methoxy-N-(pyridine-3-ylmethyl)phenylsulfonamido)acetamide |
3OHO | 2.5 | catalytic domain of stromelysin-1 in complex with N-Hydroxy-2-(4-methylphenylsulfonamido)acetamide |
3USN | STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE THIADIAZOLE INHIBITOR IPNU-107859, NMR, 1 STRUCTURE | |
4DPE | 1.96 | Structure of MMP3 complexed with a platinum-based inhibitor. |
4G9L | 1.88 | Structure of MMP3 complexed with NNGH inhibitor. |
4JA1 | 1.96 | Structure of MMP3 complexed with a platinum-based inhibitor |
6MAV | 2.37 | Complex of tissue inhibitor of metalloproteinase-1 (TIMP-1) mutant L34G with matrix metalloproteinase-3 catalytic domain (MMP-3cd) |
6N9D | 2.67 | Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/L133P/L151C/G154A) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) |
7S7L | 2.34 | Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/M66S/E67Y/L133N/S155L) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) |
7S7M | 3.0 | Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/M66D/T98G/P131S/Q153N) with matrix metalloproteinase-3 catalytic domain (MMP-3cd) |
GO ontology
|
GO term | GO description |
---|---|---|
Biological Process | GO:0071492 | cellular response to UV-A |
Biological Process | GO:0071732 | cellular response to nitric oxide |
Biological Process | GO:0030574 | collagen catabolic process |
Biological Process | GO:0022617 | extracellular matrix disassembly |
Biological Process | GO:0030198 | extracellular matrix organization |
Biological Process | GO:0045087 | innate immune response |
Biological Process | GO:0010727 | negative regulation of hydrogen peroxide metabolic process |
Biological Process | GO:1903209 | positive regulation of oxidative stress-induced cell death |
Biological Process | GO:0031334 | positive regulation of protein-containing complex assembly |
Biological Process | GO:0006508 | proteolysis |
Biological Process | GO:0150077 | regulation of neuroinflammatory response |
Biological Process | GO:1904645 | response to amyloid-beta |
Molecular Function | GO:0004175 | endopeptidase activity |
Molecular Function | GO:0004222 | metalloendopeptidase activity |
Molecular Function | GO:0008237 | metallopeptidase activity |
Molecular Function | GO:0008233 | peptidase activity |
Molecular Function | GO:0004252 | serine-type endopeptidase activity |
Molecular Function | GO:0008270 | zinc ion binding |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0031012 | extracellular matrix |
Cellular Component | GO:0005576 | extracellular region |
Cellular Component | GO:0005615 | extracellular space |
Cellular Component | GO:0005634 | nucleus |
InterPro
|
InterPro name |
---|---|
IPR000585 | Hemopexin-like domain |
IPR001818 | Peptidase M10, metallopeptidase |
IPR002477 | Peptidoglycan binding-like |
IPR006026 | Peptidase, metallopeptidase |
IPR018486 | Hemopexin, conserved site |
IPR018487 | Hemopexin-like repeats |
IPR021158 | Peptidase M10A, cysteine switch, zinc binding site |
IPR021190 | Peptidase M10A |
IPR024079 | Metallopeptidase, catalytic domain superfamily |
IPR033739 | Peptidase M10A, catalytic domain |
IPR036365 | PGBD-like superfamily |
IPR036375 | Hemopexin-like domain superfamily |
Pfam
|
Pfam name |
---|---|
PF00045 | Hemopexin |
PF00413 | Matrixin |
PF01471 | Putative peptidoglycan binding domain |
Reactome
|
Reactome Name | Node type
|
Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-1442490 | Collagen degradation | Leaf | R-HSA-1474244 | Extracellular matrix organization |
R-HSA-1474228 | Degradation of the extracellular matrix | Internal node | R-HSA-1474244 | Extracellular matrix organization |
R-HSA-1592389 | Activation of Matrix Metalloproteinases | Leaf | R-HSA-1474244 | Extracellular matrix organization |
R-HSA-2022090 | Assembly of collagen fibrils and other multimeric structures | Internal node | R-HSA-1474244 | Extracellular matrix organization |
R-HSA-2179392 | EGFR Transactivation by Gastrin | Leaf | R-HSA-162582 | Signal Transduction |
R-HSA-6785807 | Interleukin-4 and Interleukin-13 signaling | Leaf | R-HSA-168256 | Immune System |
R-HSA-9009391 | Extra-nuclear estrogen signaling | Internal node | R-HSA-162582 | Signal Transduction |
Location
|
ECO term
|
Pubmed |
---|---|---|
Cytoplasm | ECO:0000269 | PubMed:35940311 |
Nucleus | ECO:0000269 | PubMed:35940311 |
Secreted, extracellular space, extracellular matrix |
Disease name | MONDO ID
|
ICD10
|
ICD10 chapter
|
OMIM
|
Orphanet
|
---|---|---|---|---|---|
coronary heart disease- susceptibility to- 6 | MONDO:0013765 | I25 | chapter9, Diseases of the circulatory system | OMIM:614466 |