P04264: Keratin, type II cytoskeletal 1 (KRT1)

Keratin, type II cytoskeletal 1 (KRT1) is a 644-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04264.

Gene
KRT1
Organism
Homo sapiens
Length
644 residues
Mean pLDDT
63.1
Model
AF-P04264-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.1 (low 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 accurate28%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions49%

What pLDDT means and how to read it

Function

Structural component of intermediate filaments in suprabasal keratinocytes of stratified epithelia. Forms heteropolymers with a type I keratin, assembling into keratin intermediate filament networks that provide mechanical strength and structural stability to differentiating epidermal cells (PubMed:1381288). May regulate the activity of kinases such as PKC and SRC by interacting with integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1) (PubMed:17956333, PubMed:21544310). In complex with C1QBP, acts as a high-affinity receptor for kininogen-1 (HMWK) (PubMed:21544310)

Subunit structure

Heterodimers composed of one type I and one type II keratins; forms parallel coiled-coil heterodimers (PubMed:24940650, PubMed:27595935). Heterodimers associate in an antiparallel manner to form heterotetramers, which further assemble into higher-order keratin intermediate filaments (PubMed:24940650, PubMed:27595935). Forms a heterodimer with KRT10 (PubMed:24940650, PubMed:27595935). Forms a…

Subcellular location

Cell membrane, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6UUIX-ray2.07 ÅC=370-489
6E2JX-ray2.39 ÅA=226-331
4ZRYX-ray3.3 ÅB=370-489

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