2BZ2: NELF E RRM

Solution structure of NELF E RRM. Determined by solution NMR. Released 16 Aug 2006.

Method
Solution NMR
Organism
HOMO SAPIENS
Chains
1
Atoms
610
Mol. weight
13.38 kDa
Released
16 Aug 2006

Explore 2BZ2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand41-4551
α-helix51-588
β-strand67-7041
β-strand75-7951
α-helix83-9311
β-strand9712
β-strand10212
β-strand104-10741

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Negative elongation factor EAprotein121HOMO SAPIENSP18615 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2BZ2_1 NEGATIVE ELONGATION FACTOR E (chains A)
MGSSHHHHHHSSGLVPRGSHMGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSP
FGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGK
S

Primary citation

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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