The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2. Determined by solution NMR. Released 20 Feb 2002.
Explore 1KS0 in 3D Show helices and sheets RCSB PDB PDBe
1KS0 contains 1 α-helix and 7 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 |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| β-strand | 18-20 | 3 | 2 |
| β-strand | 23-25 | 3 | 2 |
| β-strand | 29 | 1 | 1 |
| β-strand | 39-41 | 3 | 1 |
| β-strand | 45 | 1 | 2 |
| α-helix | 46-49 | 4 | |
| β-strand | 52-54 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Matrix Metalloproteinase 2 | A | protein | 63 | Homo sapiens | P08253 (AlphaFold model) |
>1KS0_1 Matrix Metalloproteinase 2 (chains A) RIPVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEAL FTM
The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains. Gehrmann, M., Briknarova, K., Banyai, L. et al. Biol Chem (2002) 383:137-148. DOI 10.1515/BC.2002.014 · PubMed
Other PDB entries of the same protein (UniProt P08253 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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