Keratin 14 120 - 144 peptide fragment. Determined by solution NMR. Released 24 Jun 2026.
Explore 9VHS in 3D Show helices and sheets RCSB PDB PDBe
9VHS contains 1 α-helix 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 | 10-15 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Keratin, type I cytoskeletal 14 | A | protein | 25 | Homo sapiens | P02533 (AlphaFold model) |
>9VHS_1 Keratin, type I cytoskeletal 14 (chains A) QNLNDRLASYLDKVRALEEANADLE
Conformational Compactness Dictates Aggregation Propensity: Single-Point Mutations Reshape Energy Landscapes and Self-Assembly Pathways of a Keratin Peptide. Zhang, W.B., Li, Z.Y., Li, H.W. et al. To be published.
Other PDB entries of the same protein (UniProt P02533 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9VHS directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.