Card domain from apaf-1. Determined by X-ray diffraction at 1.6 Å resolution. Released 19 Apr 2000.
Explore 2YGS in 3D Show helices and sheets RCSB PDB PDBe
2YGS contains 6 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 | 3-19 | 17 | |
| α-helix | 23-32 | 10 | |
| α-helix | 37-44 | 8 | |
| α-helix | 49-60 | 12 | |
| α-helix | 65-77 | 13 | |
| α-helix | 81-88 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptotic protease activating factor 1 | A | protein | 92 | Homo sapiens | O14727 (AlphaFold model) |
>2YGS_1 APOPTOTIC PROTEASE ACTIVATING FACTOR 1 (chains A) MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI LKKDNDSYVSFYNALLHEGYKDLAALLHDGIP
Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Qin, H., Srinivasula, S.M., Wu, G. et al. Nature (1999) 399:549-557. DOI 10.1038/21124 · 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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