Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker. Determined by solution NMR. Released 8 Sept 2009.
Explore 2KIS in 3D Show helices and sheets RCSB PDB PDBe
2KIS contains 4 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 | 618-632 | 15 | |
| α-helix | 642-648 | 7 | |
| α-helix | 651-654 | 4 | |
| α-helix | 660-680 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation regulator 1 | A | protein | 71 | Homo sapiens | O14776 (AlphaFold model) |
>2KIS_1 Transcription elongation regulator 1 (chains A) GAMGSLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTR AEEERREKKNK
Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. Murphy, J.M., Hansen, D.F., Wiesner, S. et al. J Mol Biol (2009) 393:409-424. DOI 10.1016/j.jmb.2009.08.049 · PubMed
Other PDB entries of the same protein (UniProt O14776 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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