3.4.24.22: stromelysin 2

This is an abbreviated version!
For detailed information about stromelysin 2, go to the full flat file.

Reaction

Similar to stromelysin 1, but action on collagen types III, IV and V is weak =

Synonyms

Matrix metalloproteinase 10, Matrix metalloproteinase-10, MMP-10, MMP10, More, Proteoglycanase 2, ST-2, stromelysin 2, stromelysin-2, Transformation-associated protein 34A, Transin 2, Transins, 2

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.22 stromelysin 2

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	Activating Compound
8	AA Sequence
7	Application
1	CAS Registry Number
11	Cloned(Commentary)
3	Crystallization (Commentary)
1174	Disease/ Diagnostics
14	Expression
50	General Information
22	Inhibitors
3	Ki Value [mM]
2	KM Value [mM]
19	Localization
10	Metals/Ions
3	Molecular Weight [Da]
16	Natural Substrates/ Products (Substrates)
54	Organism
6	PDB ID
4	pH Optimum
1	pH Range
4	Posttranslational Modification
8	Protein Variants
2	Purification (Commentary)
1	Reaction
1	Reaction Type
49	Reference
94	Source Tissue
2	Storage Stability
43	Substrates and Products (Substrate)
1	Subunits
73	Synonyms
2	Temperature Optimum [°C]
1	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Crystallization on EC 3.4.24.22 - stromelysin 2

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified active human MMP-10 catalytic domain in complex with inhibitor protein TIMP-2, hanging drop vapor diffusion method, mixing of proteins in a 1:1.1 (mol/mol) ratio, 4.5-5.5 mg/ml protein in 20 mM Tris, pH 8.5 and 150 mM NaCl, are mixed with reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% w/v PEG 2000 monomethyl ether, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement, comparison and analysis of the crystal structure of the human MMP-10/TIMP-1 complex, PDB ID 3V96

Homo sapiens

P16035

735101

purified isolated catalytic enzyme domain in complex with inhibitor TIMP1, 1:1.2 (mol/mol) mixture of enzyme protein and fully deglycosylated TIMP-N30A mutant is concentrated to achieve a final protein concentration of 4-5 mg/ml. Crystals are grown by hanging drop vapor diffusion method at room temperature in 0.1 M sodium dihydrogen phosphate, pH 6.5, 12% w/v PEG 8000, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement

Homo sapiens

P01033

734175

recombinant catalytic domain, in complex with inhibitor N-isobutyl-N-(4-methoxy-phenylsulfonyl)glycyl hydroxamic acid, i.e. NNGH. Comparison with structure of matrix metalloproteinase MMP-3

Homo sapiens

-

669828