Q8VDS3: Chromobox protein homolog 7 (Cbx7)

Chromobox protein homolog 7 (Cbx7) is a 158-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8VDS3.

Gene
Cbx7
Organism
Mus musculus
Length
158 residues
Mean pLDDT
74.2
Model
AF-Q8VDS3-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.2 (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 accurate36%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution35%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:16537902, PubMed:22226355). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3) (By similarity). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (PubMed:16537902, PubMed:22226355). Trimethylation at 'Lys-27' (H3K27me3) is important for chromatin…

Subunit structure

Component of a PRC1-like complex (PubMed:22226355). Distinct PRC1-like core complexes are composed of a RING1 subunit (RING1B or RING1A), one of the six PCGF proteins (PCGF1-6), one PHC protein (PHC1-3) and one of the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8) (PubMed:22226355). The composition of the PRC1 complex may differ between the PRC1 complex in pluripotent embryonic stem cells…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4X3KX-ray1.45 ÅA/B=7-66
4X3SX-ray1.6 ÅA/B=7-66
4X3UX-ray1.63 ÅA/B=7-66
4X3TX-ray2.14 ÅA/B/C/D/E/F=7-66
5EJWX-ray2.6 ÅA=1-71
2KVMNMRA=1-71

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