Elongation factor tfiis domain II. Determined by solution NMR. Released 12 Apr 2000.
Explore 1ENW in 3D Show helices and sheets RCSB PDB PDBe
1ENW contains 7 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 | 23-37 | 15 | |
| α-helix | 45-52 | 8 | |
| α-helix | 66-70 | 5 | |
| α-helix | 71-75 | 5 | |
| α-helix | 76-80 | 5 | |
| α-helix | 91-94 | 4 | |
| α-helix | 102-105 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation factor S-II | A | protein | 114 | Saccharomyces cerevisiae | P07273 (AlphaFold model) |
>1ENW_1 TRANSCRIPTION ELONGATION FACTOR S-II (chains A) GSHMPRNSKNDGVDTAIYHHKLRDQVLKALYDVLAKESEHPPQSILHTAKAIESEMNKVN NCDTNEAAYKARYRIIYSNVISKNNPDLKHKIANGDITPEFLATCDAKDLAPAP
Elongation factor TFIIS contains three structural domains: solution structure of domain II. Morin, P.E., Awrey, D.E., Edwards, A.M. et al. Proc Natl Acad Sci U S A (1996) 93:10604-10608. DOI 10.1073/pnas.93.20.10604 · PubMed
Other PDB entries of the same protein (UniProt P07273 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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