Solution structure of the FF Domain 2 of human transcription elongation factor CA150. Determined by solution NMR. Released 28 Jul 2009.
Explore 2KIQ in 3D Show helices and sheets RCSB PDB PDBe
2KIQ 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 | 7-18 | 12 | |
| α-helix | 27-34 | 8 | |
| α-helix | 38-42 | 5 | |
| α-helix | 46-60 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation regulator 1 | A | protein | 62 | Homo sapiens | O14776 (AlphaFold model) |
>2KIQ_1 Transcription elongation regulator 1 (chains A) SHMKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAA RK
High-resolution protein structure determination starting with a global fold calculated from exact solutions to the RDC equations. Zeng, J., Boyles, J., Tripathy, C. et al. J Biomol NMR (2009) 45:265-281. DOI 10.1007/s10858-009-9366-3 · 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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