matrix metalloproteinase-10 proenzyme. Determined by X-ray diffraction at 1.67 Å resolution. Released 13 Aug 2025.
Explore 9CSX in 3D Show helices and sheets RCSB PDB PDBe
9CSX contains 7 α-helices and 10 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 27-41 | 15 | |
| α-helix | 57-70 | 14 | |
| α-helix | 80-87 | 8 | |
| β-strand | 90 | 1 | 1 |
| β-strand | 112-117 | 6 | 2 |
| α-helix | 126-141 | 16 | |
| β-strand | 147-150 | 4 | 2 |
| β-strand | 158-163 | 6 | 2 |
| β-strand | 179 | 1 | 1 |
| β-strand | 181-183 | 3 | 2 |
| β-strand | 194-197 | 4 | 2 |
| β-strand | 202-203 | 2 | 3 |
| β-strand | 209-210 | 2 | 3 |
| α-helix | 211-223 | 13 | |
| β-strand | 238 | 1 | 1 |
| α-helix | 245-247 | 3 | |
| α-helix | 252-262 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Stromelysin-2 | A | protein | 274 | Homo sapiens | P09238 (AlphaFold model) |
>9CSX_1 Stromelysin-2 (chains A) YPLSGAAKEEDSNKDLAQQYLEKYYNLEKDVKQFRRKDSNLIVKKIQGMQKFLGLEVTGK LDTDTLEVMRKPRCGVPDVGHFSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKAL KVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFD DDEKWTEDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNG IQSLYGPPPASTEEPLVPTKSVPSGSEMPAKCDP
Water and common crystallization additives (ACY, IMD) are not listed.
Matrix metalloproteinase-10 (MMP-10) proenzyme. Isiorho, E.A. To be published.
Other PDB entries of the same protein (UniProt P09238 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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