Solution structure of NELF E RRM. Determined by solution NMR. Released 16 Aug 2006.
Explore 2BZ2 in 3D Show helices and sheets RCSB PDB PDBe
2BZ2 contains 2 α-helices and 6 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 | 41-45 | 5 | 1 |
| α-helix | 51-58 | 8 | |
| β-strand | 67-70 | 4 | 1 |
| β-strand | 75-79 | 5 | 1 |
| α-helix | 83-93 | 11 | |
| β-strand | 97 | 1 | 2 |
| β-strand | 102 | 1 | 2 |
| β-strand | 104-107 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Negative elongation factor E | A | protein | 121 | HOMO SAPIENS | P18615 (AlphaFold model) |
>2BZ2_1 NEGATIVE ELONGATION FACTOR E (chains A) MGSSHHHHHHSSGLVPRGSHMGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSP FGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGK S
Structural studies on the RNA-recognition motif of NELF E, a cellular negative transcription elongation factor involved in the regulation of HIV transcription. Rao, J.N., Neumann, L., Wenzel, S. et al. Biochem J (2006) 400:449-456. DOI 10.1042/BJ20060421 · PubMed
Other PDB entries of the same protein (UniProt P18615 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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