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NIH3D

Secondary Structure - 3-10 Helix

Generated by NIH 3D workflows using data provided by
phil.cruz
Created:
3/13/15
Submitted:
3/6/23
Published:
3/6/23

Select an image below to view

3DPX-001189

Licensing:

Public Domain
706
44
Version 2

Category

Biomacromolecules
Biomacromolecules
Description

An alpha helix is a commonly-found protein secondary structure. It is a right-handed coil in which every backbone N-H group donates a hydrogen bond to the C=O group of the amino acid four residues earlier. In the less common 3-10 helix, the bonding occurs at the amino acid three residues earlier, resulting in a tighter helical conformation.

This helix consists of 20 amino acid peptides of poly-L-alanine, and were produced using the peptide builder in Chimera. Phi angle is set at -49.0, and psi angle is set at -26.0.



Download the .pdb file here.

3-10 helix

by tjwatt


3-10 helix