Crystal structure of the apaf-1 card. Determined by X-ray diffraction at 1.3 Å resolution. Released 13 Sept 1999.
Explore 1CY5 in 3D Show helices and sheets RCSB PDB PDBe
1CY5 contains 8 α-helices and 0 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 | 3-11 | 9 | |
| α-helix | 13-19 | 7 | |
| α-helix | 22-32 | 11 | |
| α-helix | 37-44 | 8 | |
| α-helix | 49-61 | 13 | |
| α-helix | 65-77 | 13 | |
| α-helix | 81-87 | 7 | |
| α-helix | 88-90 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (apoptotic protease activating factor 1) | A | protein | 97 | Homo sapiens | O14727 (AlphaFold model) |
>1CY5_1 PROTEIN (APOPTOTIC PROTEASE ACTIVATING FACTOR 1) (chains A) MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 5 |
Water and common crystallization additives (BME) are not listed.
Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling. Vaughn, D.E., Rodriguez, J., Lazebnik, Y. et al. J Mol Biol (1999) 293:439-447. DOI 10.1006/jmbi.1999.3177 · PubMed
Other PDB entries of the same protein (UniProt O14727 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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