9VHO: Keratin 14 120 - 144 peptide fragment

Keratin 14 120 - 144 peptide fragment (R125H). Determined by solution NMR. Released 24 Jun 2026.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
200
Mol. weight
2.85 kDa
Released
24 Jun 2026

Explore 9VHO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VHO 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.

Chain A: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix10-189

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Keratin, type I cytoskeletal 14Aprotein25Homo sapiensP02533 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9VHO_1 Keratin, type I cytoskeletal 14 (chains A)
QNLNDHLASYLDKVRALEEANADLE

Primary citation

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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