Keratin 14 120 - 144 peptide fragment (R125G). Determined by solution NMR. Released 24 Jun 2026.
Explore 9VHF in 3D Show helices and sheets RCSB PDB PDBe
9VHF 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 | 9-16 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Keratin, type I cytoskeletal 14 | A | protein | 25 | Homo sapiens | P02533 (AlphaFold model) |
>9VHF_1 Keratin, type I cytoskeletal 14 (chains A) QNLNDGLASYLDKVRALEEANADLE
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:
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