Structure of cleaved, CARD domain deleted Caspase-9. Determined by X-ray diffraction at 2.8 Å resolution. Released 12 Dec 2001.
Explore 1JXQ in 3D Show helices and sheets RCSB PDB PDBe
1JXQ contains 33 α-helices and 70 β-strands across 6 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 | 141-147 | 7 | |
| β-strand | 152-153 | 2 | 1 |
| β-strand | 163-169 | 7 | 2 |
| α-helix | 176-178 | 3 | |
| α-helix | 182-195 | 14 | |
| β-strand | 198-204 | 7 | 2 |
| α-helix | 208-219 | 12 | |
| β-strand | 229-235 | 7 | 2 |
| β-strand | 238-239 | 2 | 3 |
| β-strand | 240C | 1 | 4 |
| β-strand | 242-244 | 3 | 3 |
| β-strand | 255-257 | 3 | 3 |
| α-helix | 258-264 | 7 | |
| α-helix | 271-273 | 3 | |
| β-strand | 278-283 | 6 | 2 |
| β-strand | 289 | 1 | 5 |
| β-strand | 291 | 1 | 6 |
| β-strand | 294-295 | 2 | 7 |
| β-strand | 327-331 | 5 | 2 |
| β-strand | 337 | 1 | 5 |
| α-helix | 338-339 | 2 | |
| β-strand | 340 | 1 | 8 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-378 | 13 | |
| β-strand | 384 | 1 | 6 |
| β-strand | 388-393 | 5 | 2 |
| β-strand | 397-398 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 152 | 1 | 9 |
| β-strand | 163-169 | 7 | 2 |
| α-helix | 176-178 | 3 | |
| α-helix | 182-195 | 14 | |
| β-strand | 198-204 | 7 | 2 |
| α-helix | 208-219 | 12 | |
| β-strand | 229-236 | 8 | 2 |
| β-strand | 238 | 1 | 10 |
| β-strand | 240C | 1 | 4 |
| β-strand | 242-244 | 3 | 10 |
| β-strand | 255-257 | 3 | 10 |
| α-helix | 258-263 | 6 | |
| α-helix | 271-273 | 3 | |
| β-strand | 278-284 | 7 | 2 |
| β-strand | 320-321 | 2 | 7 |
| β-strand | 327-332 | 6 | 2 |
| β-strand | 337 | 1 | 11 |
| β-strand | 347 | 1 | 11 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-380 | 15 | |
| β-strand | 388-393 | 5 | 2 |
| β-strand | 397 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 141-147 | 7 | |
| β-strand | 152-153 | 2 | 12 |
| β-strand | 163-169 | 7 | 13 |
| α-helix | 176-178 | 3 | |
| α-helix | 182-195 | 14 | |
| β-strand | 198-204 | 7 | 13 |
| α-helix | 208-220 | 13 | |
| β-strand | 229-235 | 7 | 13 |
| β-strand | 238-239 | 2 | 14 |
| β-strand | 240C | 1 | 15 |
| β-strand | 242-244 | 3 | 14 |
| β-strand | 255-257 | 3 | 14 |
| α-helix | 258-263 | 6 | |
| α-helix | 271-273 | 3 | |
| β-strand | 278-283 | 6 | 13 |
| β-strand | 289 | 1 | 16 |
| β-strand | 291 | 1 | 17 |
| β-strand | 294-295 | 2 | 18 |
| β-strand | 327-331 | 5 | 13 |
| β-strand | 337 | 1 | 16 |
| α-helix | 338-339 | 2 | |
| β-strand | 340 | 1 | 19 |
| β-strand | 341-342 | 2 | 20 |
| β-strand | 346-347 | 2 | 20 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-377 | 12 | |
| β-strand | 384 | 1 | 17 |
| β-strand | 388-393 | 5 | 13 |
| β-strand | 397-398 | 2 | 12 |
| α-helix | 400-402 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 152 | 1 | 21 |
| β-strand | 163-169 | 7 | 13 |
| α-helix | 176-178 | 3 | |
| α-helix | 182-195 | 14 | |
| β-strand | 198-204 | 7 | 13 |
| α-helix | 208-219 | 12 | |
| β-strand | 229-236 | 8 | 13 |
| β-strand | 238 | 1 | 22 |
| β-strand | 240C | 1 | 15 |
| β-strand | 242-244 | 3 | 22 |
| β-strand | 255-257 | 3 | 22 |
| α-helix | 258-263 | 6 | |
| α-helix | 271-273 | 3 | |
| β-strand | 278-284 | 7 | 13 |
| β-strand | 320-321 | 2 | 18 |
| β-strand | 327-332 | 6 | 13 |
| β-strand | 337-339 | 3 | 23 |
| β-strand | 342-347 | 6 | 23 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-378 | 13 | |
| β-strand | 388-393 | 5 | 13 |
| β-strand | 397 | 1 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 504 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Caspase-9 | A, B, C, D | protein | 284 | Homo sapiens | P55211 (AlphaFold model) |
| benzoxycarbonyl-Val-Ala-Asp-fluoromethyl ketone Inhibitor | E, F | protein | 5 |
>1JXQ_1 Caspase-9 (chains A, B, C, D) MGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLH FMVEVKGDLTAKKMVLALLELARQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPV SVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATP FQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSE DLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTSHHHHHH
>1JXQ_2 benzoxycarbonyl-Val-Ala-Asp-fluoromethyl ketone Inhibitor (chains E, F) XEVDX
Dimer formation drives the activation of the cell death protease caspase 9. Renatus, M., Stennicke, H.R., Scott, F.L. et al. Proc Natl Acad Sci U S A (2001) 98:14250-14255. DOI 10.1073/pnas.231465798 · PubMed
Other PDB entries of the same protein (UniProt P55211 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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