Crystal structure of human caspase-9 CARD. Determined by X-ray diffraction at 2.46 Å resolution. Released 20 May 2026.
Explore 9R44 in 3D Show helices and sheets RCSB PDB PDBe
9R44 contains 29 α-helices and 0 β-strands across 4 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 | 3-11 | 9 | |
| α-helix | 13-19 | 7 | |
| α-helix | 25-31 | 7 | |
| α-helix | 37-44 | 8 | |
| α-helix | 51-62 | 12 | |
| α-helix | 69-79 | 11 | |
| α-helix | 83-94 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-11 | 9 | |
| α-helix | 13-19 | 7 | |
| α-helix | 25-31 | 7 | |
| α-helix | 37-44 | 8 | |
| α-helix | 51-62 | 12 | |
| α-helix | 69-78 | 10 | |
| α-helix | 83-93 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-11 | 9 | |
| α-helix | 13-19 | 7 | |
| α-helix | 22-24 | 3 | |
| α-helix | 26-31 | 6 | |
| α-helix | 37-44 | 8 | |
| α-helix | 51-62 | 12 | |
| α-helix | 69-79 | 11 | |
| α-helix | 83-93 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-11 | 9 | |
| α-helix | 13-19 | 7 | |
| α-helix | 25-31 | 7 | |
| α-helix | 37-44 | 8 | |
| α-helix | 51-62 | 12 | |
| α-helix | 69-79 | 11 | |
| α-helix | 83-98 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Caspase-9 | A, E, H, L | protein | 101 | Homo sapiens | P55211 (AlphaFold model) |
>9R44_1 Caspase-9 (chains A, E, H, L) SGMDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQL IIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLS
Mechanistic insights into the caspase-9 CARD oligomerization. Rawal, S., Bohn, S., Pavkov-Keller, T. et al. To be published.
Other PDB entries of the same protein (UniProt P55211 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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