The second type II module from human matrix metalloproteinase 2. Determined by solution NMR. Released 12 Nov 1999.
Explore 1CXW in 3D Show helices and sheets RCSB PDB PDBe
1CXW contains 2 α-helices and 6 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 | 13-15 | 3 | |
| β-strand | 19-21 | 3 | 1 |
| β-strand | 24-26 | 3 | 1 |
| β-strand | 30 | 1 | 2 |
| β-strand | 39-42 | 4 | 2 |
| β-strand | 46 | 1 | 1 |
| α-helix | 47-50 | 4 | |
| β-strand | 53-56 | 4 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human matrix metalloproteinase 2 | A | protein | 60 | Homo sapiens | P08253 (AlphaFold model) |
>1CXW_1 HUMAN MATRIX METALLOPROTEINASE 2 (chains A) TALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETA
The second type II module from human matrix metalloproteinase 2: structure, function and dynamics. Briknarova, K., Grishaev, A., Banyai, L. et al. Structure (1999) 7:1235-1245. DOI 10.1016/S0969-2126(00)80057-X · 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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