Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor. Determined by X-ray diffraction at 2.02 Å resolution. Released 27 Jun 2006.
Explore 2D1O in 3D Show helices and sheets RCSB PDB PDBe
2D1O contains 8 α-helices and 20 β-strands across 2 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 | 85 | 1 | 1 |
| β-strand | 96-101 | 6 | 2 |
| α-helix | 110-125 | 16 | |
| β-strand | 131-134 | 4 | 2 |
| β-strand | 142-147 | 6 | 2 |
| β-strand | 165-167 | 3 | 2 |
| β-strand | 178-181 | 4 | 2 |
| β-strand | 186-187 | 2 | 3 |
| β-strand | 193-194 | 2 | 3 |
| α-helix | 195-206 | 12 | |
| β-strand | 209 | 1 | 1 |
| β-strand | 227 | 1 | 4 |
| α-helix | 229-231 | 3 | |
| α-helix | 236-246 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 85 | 1 | 5 |
| β-strand | 96-101 | 6 | 6 |
| α-helix | 110-125 | 16 | |
| β-strand | 131-134 | 4 | 6 |
| β-strand | 142-147 | 6 | 6 |
| β-strand | 165-167 | 3 | 6 |
| β-strand | 178-181 | 4 | 6 |
| β-strand | 186-187 | 2 | 7 |
| β-strand | 193-194 | 2 | 7 |
| α-helix | 195-207 | 13 | |
| β-strand | 209 | 1 | 5 |
| β-strand | 227 | 1 | 4 |
| α-helix | 229-231 | 3 | |
| α-helix | 236-246 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Stromelysin-1 | A, B | protein | 171 | Homo sapiens | P08254 (AlphaFold model) |
>2D1O_1 Stromelysin-1 (chains A, B) FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHE IGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSP
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453. Kohno, T., Hochigai, H., Yamashita, E. et al. Biochem Biophys Res Commun (2006) 344:315-322. DOI 10.1016/j.bbrc.2006.03.098 · PubMed
Other PDB entries of the same protein (UniProt P08254 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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