O95619: YEATS domain-containing protein 4 (YEATS4)

YEATS domain-containing protein 4 (YEATS4) is a 227-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O95619.

Gene
YEATS4
Organism
Homo sapiens
Length
227 residues
Mean pLDDT
91.6
Model
AF-O95619-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.6 (very high 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 accurate80%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Chromatin reader component of the NuA4 histone acetyltransferase (HAT) complex, a complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:12963728, PubMed:14966270). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac) (PubMed:29437725, PubMed:29900004, PubMed:30071723). Also able to recognize and bind crotonylated histone H3 (PubMed:30071723). May also recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ); additional evidence is…

Subunit structure

Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity (PubMed:12963728, PubMed:14966270). Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8IJ0X-ray1.52 ÅA/B=19-159
7EIFX-ray1.58 ÅA=19-159
5R68X-ray1.64 ÅA/B=18-190
9X8SX-ray1.7 ÅA/B/C/D=15-146
5R69X-ray1.83 ÅA/B=18-190
5VNAX-ray2.1 ÅA/B/C/D=1-148
5XTZX-ray2.1 ÅA/B/C/D=15-159
7JFYX-ray2.1 ÅA/B/C/D=1-148
8IIZX-ray2.1 ÅA=19-159
8IIYX-ray2.15 ÅA=19-159
8I60X-ray2.3 ÅC/D=11-150
9O4YX-ray2.3 ÅA/B/C/D=1-148
5VNBX-ray2.4 ÅA/B/C/D=1-148
8DKBX-ray2.58 ÅA/B/C/D/E/F/G/H=1-149
5Y8VX-ray2.61 ÅA/B/C/D=21-160
9X8UX-ray3.0 ÅA/B/C/D=15-145
8X15EM3.2 ÅW=1-227
8X19EM3.2 ÅW=1-227
8X1CEM3.2 ÅW=1-227

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