Crystal structure of MMP3 complexed with a modified proline scaffold based inhibitor. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Oct 2000.
Explore 1D7X in 3D Show helices and sheets RCSB PDB PDBe
1D7X contains 6 α-helices and 18 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 | 84 | 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 | 195-207 | 13 | |
| β-strand | 210 | 1 | 1 |
| α-helix | 236-246 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 584-585 | 2 | 4 |
| β-strand | 596-601 | 6 | 5 |
| α-helix | 610-625 | 16 | |
| β-strand | 631-634 | 4 | 5 |
| β-strand | 642-647 | 6 | 5 |
| β-strand | 665-667 | 3 | 5 |
| β-strand | 678-681 | 4 | 5 |
| β-strand | 686-687 | 2 | 6 |
| β-strand | 693-694 | 2 | 6 |
| α-helix | 695-706 | 12 | |
| β-strand | 709-710 | 2 | 4 |
| α-helix | 736-746 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Stromelysin-1 precursor | A, B | protein | 173 | Homo sapiens | P08254 (AlphaFold model) |
>1D7X_1 STROMELYSIN-1 PRECURSOR (chains A, B) FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHE IGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPET
| ID | Name | Formula | Copies |
|---|---|---|---|
| SPC | N-hydroxy 1N(4-methoxyphenyl)sulfonyl-4-(z,e-N-methoxyimino)pyrrolidine-2R-carb… | C13 H19 N3 O6 S | 2 |
| CA | Calcium ion | Ca | 6 |
| ZN | Zinc ion | Zn | 4 |
Design, synthesis, and biological evaluation of matrix metalloproteinase inhibitors derived from a modified proline scaffold. Cheng, M., De, B., Almstead, N.G. et al. J Med Chem (1999) 42:5426-5436. DOI 10.1021/jm9904699 · 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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