Q13185: Chromobox protein homolog 3 (CBX3)

Chromobox protein homolog 3 (CBX3) is a 183-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13185.

Gene
CBX3
Organism
Homo sapiens
Length
183 residues
Mean pLDDT
75.4
Model
AF-Q13185-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.4 (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 accurate25%
70 to 90Confident: backbone generally right41%
50 to 70Low: treat with caution22%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Component of heterochromatin, which recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression (PubMed:11242053). Also recognizes and binds histone H1.4 methylated at 'Lys-26' (H1.4K26me) (PubMed:16127177). Excluded from chromatin when histone H1.4 is Simultaneously methylated at Lys-26 (H1.4K26me) and phosphorylated at Ser-27 (H1.4S27Ph) (PubMed:16127177). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (PubMed:15502821). Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases…

Subunit structure

Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9' (PubMed:11242053). Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with INCENP, TRIM28/TIF1B, KMT5B, KMT5C and SP100 (PubMed:10330177, PubMed:12004135, PubMed:9636146). Interacts with TIF1A (By similarity). Interacts with…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5T1IX-ray1.6 ÅA/B=110-176
3KUPX-ray1.77 ÅA/B/C/D=110-173
9OSCX-ray1.77 ÅA=110-176
8JZWX-ray1.8 ÅA/B/C/D=110-182
3TZDX-ray1.81 ÅA=29-81
6HW2X-ray1.94 ÅB/C=109-183
3DM1X-ray2.4 ÅA/C/E/G=29-86
2L11NMRA=29-81

More AlphaFold highlights

About this viewer

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