NMR structure of apo cbfb. Determined by solution NMR. Released 26 Sept 2001.
Explore 1ILF in 3D Show helices and sheets RCSB PDB PDBe
1ILF contains 5 α-helices and 7 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 | 8-14 | 7 | |
| α-helix | 16-22 | 7 | |
| β-strand | 24-29 | 6 | 1 |
| α-helix | 37-47 | 11 | |
| α-helix | 48-50 | 3 | |
| β-strand | 52-57 | 6 | 1 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 86 | 1 | 1 |
| β-strand | 95-103 | 9 | 1 |
| β-strand | 106-114 | 9 | 1 |
| β-strand | 120-127 | 8 | 1 |
| α-helix | 129-139 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Core-binding factor | A | protein | 141 | Mus musculus | Q08024 (AlphaFold model) |
>1ILF_1 CORE-BINDING FACTOR (chains A) MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQTRFQNACRDGRSEIAFVAT GTNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLHRLD GMGCLEFDEERAQQEDALAQQ
Structure and backbone dynamics of Apo-CBFbeta in solution. Wolf-Watz, M., Grundstrom, T., Hard, T. Biochemistry (2001) 40:11423-11432. DOI 10.1021/bi010713+ · PubMed
Other PDB entries of the same protein (UniProt Q08024 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1ILF 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.