P10412: Histone H1.4 (H1-4)

Histone H1.4 (H1-4) is a 219-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10412.

Gene
H1-4
Organism
Homo sapiens
Length
219 residues
Mean pLDDT
64.8
Model
AF-P10412-F1 v6
Model created
1 Aug 2025
PDB structures
26

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Model confidence (pLDDT)

The mean pLDDT of this model is 64.8 (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 accurate31%
70 to 90Confident: backbone generally right2%
50 to 70Low: treat with caution35%
Below 50Very low: often disordered regions32%

What pLDDT means and how to read it

Function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:35581345, PubMed:40240600). Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers and promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 complex (PubMed:35581345, PubMed:40240600, PubMed:40516528). Ability to associate with nucleosomes and compact chromatin depends on linker DNA length and trajectory (PubMed:35581345). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:40240600)

Subunit structure

Associates with nucleosomes, promoting condensation into higher-order structured chromatin

Subcellular location

Nucleus, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3TZDX-ray1.81 ÅT=19-36
6H8PX-ray1.98 ÅC/D=18-32
5JJZX-ray2.0 ÅB=21-32
7K5YEM2.76 ÅU=1-219
8H1TEM3.0 ÅK=1-219
7K63EM3.03 ÅU=1-35, U=111-219
8VG2EM3.04 ÅU=1-219
9DDEEM3.2 ÅO=1-219
7PF5EM3.8 Åu=2-219
7PF3EM4.0 Ås=2-219
7PF6EM4.0 ÅU=2-219
7PFXEM4.3 ÅS=2-219
7PFDEM4.4 ÅU=2-219
7PFEEM4.4 Åu=2-219
7PFVEM4.4 ÅU=2-219
7PFUEM5.0 ÅS/U=2-219
7PEXEM5.1 Åu=2-219
7PF2EM5.1 ÅU=2-219
7PFWEM5.2 Åu=2-219
7PFCEM6.4 ÅU=2-219

Showing 20 of 26 experimental structures (best resolution first).

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