Solution structure of apaf-1 card. Determined by solution NMR. Released 20 Sept 1999.
Explore 1C15 in 3D Show helices and sheets RCSB PDB PDBe
1C15 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 | 24-29 | 6 | |
| α-helix | 30-34 | 5 | |
| α-helix | 38-45 | 8 | |
| α-helix | 51-63 | 13 | |
| α-helix | 66-76 | 11 | |
| α-helix | 81-88 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptotic protease activating factor 1 | A | protein | 97 | Homo sapiens | O14727 (AlphaFold model) |
>1C15_1 APOPTOTIC PROTEASE ACTIVATING FACTOR 1 (chains A) MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSS
Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction. Zhou, P., Chou, J., Olea, R.S. et al. Proc Natl Acad Sci U S A (1999) 96:11265-11270. DOI 10.1073/pnas.96.20.11265 · PubMed
Other PDB entries of the same protein (UniProt O14727 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1C15 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.