Structure of transactivation domain of cre-BP1/ATF-2, NMR, 20 structures. Determined by solution NMR. Released 15 Jun 1999.
Explore 1BHI in 3D Show helices and sheets RCSB PDB PDBe
1BHI contains 1 α-helix and 2 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 |
|---|---|---|---|
| β-strand | 7-8 | 2 | 1 |
| β-strand | 17-18 | 2 | 1 |
| α-helix | 21-32 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cre-BP1 | A | protein | 38 | Homo sapiens | P15336 (AlphaFold model) |
>1BHI_1 CRE-BP1 (chains A) MSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFG
Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain. Nagadoi, A., Nakazawa, K., Uda, H. et al. J Mol Biol (1999) 287:593-607. DOI 10.1006/jmbi.1999.2620 · PubMed
Other PDB entries of the same protein (UniProt P15336 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1BHI 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.