P02533: Keratin, type I cytoskeletal 14 (KRT14)

Keratin, type I cytoskeletal 14 (KRT14) is a 472-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02533.

Gene
KRT14
Organism
Homo sapiens
Length
472 residues
Mean pLDDT
73.3
Model
AF-P02533-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate50%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions29%

What pLDDT means and how to read it

Function

Structural component of intermediate filaments in basal keratinocytes of stratified epithelia. Forms heteropolymers with type II keratin KRT5, contributing to the keratin intermediate filament network that confers mechanical strength and structural integrity to the basal layer of the epidermis and other stratified epithelial (PubMed:11724817, PubMed:1694855, PubMed:1720261, PubMed:41511042). The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro (PubMed:11724817). Displays an antagonist role with KRT15 in basal epithelial cells,…

Subunit structure

Heterodimers composed of type I and type II keratin; forms parallel coiled-coil heterodimers (PubMed:11724817, PubMed:1694855, PubMed:22705788, PubMed:24940650). Two heterodimers associate in an antiparallel manner to form heterotetramers, which further assemble into higher-order intermediate filaments (PubMed:1694855). Forms a disulfide-linked heterodimer (via 2B domains) with KRT5 (via 2B…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6JFVX-ray2.6 ÅA/C=327-421
3TNUX-ray3.0 ÅA=295-422

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