Crystal structure of tandem FF domains. Determined by X-ray diffraction at 2.7 Å resolution. Released 18 Aug 2009.
Explore 3HFH in 3D Show helices and sheets RCSB PDB PDBe
3HFH contains 22 α-helices and 0 β-strands across 2 chains. 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 | 661-672 | 12 | |
| α-helix | 681-684 | 4 | |
| α-helix | 685-687 | 3 | |
| α-helix | 692-696 | 5 | |
| α-helix | 699-732 | 34 | |
| α-helix | 773-780 | 8 | |
| α-helix | 787-790 | 4 | |
| α-helix | 792-804 | 13 | |
| α-helix | 814-821 | 8 | |
| α-helix | 825-828 | 4 | |
| α-helix | 833-844 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 661-672 | 12 | |
| α-helix | 681-684 | 4 | |
| α-helix | 685-687 | 3 | |
| α-helix | 692-696 | 5 | |
| α-helix | 699-738 | 40 | |
| α-helix | 747-753 | 7 | |
| α-helix | 758-761 | 4 | |
| α-helix | 766-804 | 39 | |
| α-helix | 814-821 | 8 | |
| α-helix | 825-828 | 4 | |
| α-helix | 833-843 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation regulator 1 | A, B | protein | 190 | Homo sapiens | O14776 (AlphaFold model) |
>3HFH_1 Transcription elongation regulator 1 (chains A, B) GPLGSARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAE EERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNE FVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSM REDLFKQYIE
Crystal Structure of the Three Tandem FF Domains of the Transcription Elongation Regulator CA150. Lu, M., Yang, J., Ren, Z. et al. J Mol Biol (2009) 393:397-408. DOI 10.1016/j.jmb.2009.07.086 · PubMed
Other PDB entries of the same protein (UniProt O14776 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3HFH 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.