Crystal structure of human caspase-1 in complex with Ac-FLTD-CMK. Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Jun 2018.
Explore 6BZ9 in 3D Show helices and sheets RCSB PDB PDBe
6BZ9 contains 11 α-helices and 16 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 134-135 | 2 | |
| α-helix | 138-147 | 10 | |
| α-helix | 149-151 | 3 | |
| β-strand | 152 | 1 | 1 |
| β-strand | 164-169 | 6 | 2 |
| α-helix | 182-195 | 14 | |
| β-strand | 199-204 | 6 | 2 |
| α-helix | 208-219 | 12 | |
| α-helix | 222-226 | 5 | |
| β-strand | 230-235 | 6 | 2 |
| β-strand | 238 | 1 | 3 |
| β-strand | 243-244 | 2 | 3 |
| α-helix | 245 | 1 | |
| β-strand | 255-256 | 2 | 3 |
| α-helix | 258-265 | 8 | |
| α-helix | 271-273 | 3 | |
| β-strand | 278-283 | 6 | 2 |
| β-strand | 289 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 327-331 | 5 | 2 |
| β-strand | 337 | 1 | 4 |
| β-strand | 340-342 | 3 | 5 |
| β-strand | 346-347 | 2 | 5 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-376 | 11 | |
| β-strand | 388-390 | 3 | 2 |
| β-strand | 397 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Caspase-1 | A | protein | 178 | Homo sapiens | P29466 (AlphaFold model) |
| Caspase-1 | B | protein | 88 | Homo sapiens | P29466 (AlphaFold model) |
| Ac-fltd-cmk | C | protein | 6 | Homo sapiens |
>6BZ9_1 Caspase-1 (chains A) NPAMPTSSGSEGNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRR TGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGI REGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKD
>6BZ9_2 Caspase-1 (chains B) AIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFS FEQPDGRAQMPTTERVTLTRCFYLFPGH
>6BZ9_3 Ac-FLTD-CMK (chains C) XFLTDX
Mechanism of gasdermin D recognition by inflammatory caspases and their inhibition by a gasdermin D-derived peptide inhibitor. Yang, J., Liu, Z., Wang, C. et al. Proc Natl Acad Sci U S A (2018) 115:6792-6797. DOI 10.1073/pnas.1800562115 · PubMed
Other PDB entries of the same protein (UniProt P29466 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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