Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1). Determined by X-ray diffraction at 2.05 Å resolution. Released 30 Jun 2010.
Explore 3MA2 in 3D Show helices and sheets RCSB PDB PDBe
3MA2 contains 27 α-helices and 33 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 123-128 | 6 | 3 |
| α-helix | 137-153 | 17 | |
| β-strand | 158-161 | 4 | 3 |
| α-helix | 164-168 | 5 | |
| β-strand | 177-182 | 6 | 3 |
| β-strand | 198-202 | 5 | 3 |
| α-helix | 203-204 | 2 | |
| β-strand | 213-216 | 4 | 3 |
| β-strand | 221-222 | 2 | 4 |
| β-strand | 231-232 | 2 | 4 |
| α-helix | 233-245 | 13 | |
| α-helix | 247-250 | 4 | |
| β-strand | 260 | 1 | 3 |
| α-helix | 273-283 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 302-303 | 2 | 3 |
| α-helix | 304-305 | 2 | |
| α-helix | 308-314 | 7 | |
| β-strand | 317-330 | 14 | 5 |
| β-strand | 335-347 | 13 | 5 |
| β-strand | 360-364 | 5 | 5 |
| α-helix | 367-369 | 3 | |
| β-strand | 382-390 | 9 | 5 |
| β-strand | 393-395 | 3 | 5 |
| β-strand | 402-404 | 3 | 5 |
| α-helix | 405-407 | 3 | |
| α-helix | 410-414 | 5 | |
| α-helix | 415-419 | 5 | |
| α-helix | 420-422 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 302-303 | 2 | 1 |
| α-helix | 304-305 | 2 | |
| α-helix | 308-314 | 7 | |
| β-strand | 317-323 | 7 | 6 |
| β-strand | 328-330 | 3 | 7 |
| β-strand | 335-339 | 5 | 7 |
| β-strand | 340-347 | 8 | 6 |
| α-helix | 356-358 | 3 | |
| β-strand | 360-364 | 5 | 7 |
| α-helix | 367-369 | 3 | |
| β-strand | 382-387 | 6 | 6 |
| β-strand | 388-390 | 3 | 7 |
| β-strand | 393-395 | 3 | 7 |
| β-strand | 401-404 | 4 | 6 |
| α-helix | 405-407 | 3 | |
| α-helix | 410-417 | 8 | |
| α-helix | 419-421 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 123-128 | 6 | 1 |
| α-helix | 137-154 | 18 | |
| β-strand | 158-161 | 4 | 1 |
| α-helix | 164-168 | 5 | |
| α-helix | 173-175 | 3 | |
| β-strand | 177-182 | 6 | 1 |
| β-strand | 198-202 | 5 | 1 |
| α-helix | 203-204 | 2 | |
| β-strand | 213-216 | 4 | 1 |
| β-strand | 221-222 | 2 | 2 |
| β-strand | 231-232 | 2 | 2 |
| α-helix | 233-244 | 12 | |
| α-helix | 247-249 | 3 | |
| β-strand | 260 | 1 | 1 |
| α-helix | 273-283 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Matrix metalloproteinase-14 | A, D | protein | 181 | Homo sapiens | P50281 (AlphaFold model) |
| Metalloproteinase inhibitor 1 | B, C | protein | 125 | Homo sapiens | P01033 (AlphaFold model) |
>3MA2_1 Matrix metalloproteinase-14 (chains A, D) YAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGH EKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGN DIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPT K
>3MA2_2 Metalloproteinase inhibitor 1 (chains B, C) CTCAPVHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITLCSFVAPWNSLSLAQRRGFTKTY TVGCE
The Intrinsic Protein Flexibility of Endogenous Protease Inhibitor TIMP-1 Controls Its Binding Interface and Affects Its Function. Grossman, M., Tworowski, D., Dym, O. et al. Biochemistry (2010) 49:6184-6192. DOI 10.1021/bi902141x · PubMed
Other PDB entries of the same protein (UniProt P50281 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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