Q920Q2: DNA repair protein REV1 (Rev1)

DNA repair protein REV1 (Rev1) is a 1249-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q920Q2.

Gene
Rev1
Organism
Mus musculus
Length
1249 residues
Mean pLDDT
66.1
Model
AF-Q920Q2-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.1 (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 accurate39%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Bifunctional protein involved in the maintenance of genome stability through translesion DNA synthesis (TLS) and antibody diversification via somatic hypermutation (PubMed:14657033, PubMed:16476771, PubMed:22859295). Functions as a molecular adapter protein at stalled DNA replication, coordinating polymerases recruitment, selection, and switching, in a manner independent of its deoxycytidyl transferase activity (PubMed:14657033, PubMed:22859295). At the site of DNA lesion, recruits and mediates the switch between low-fidelity inserter DNA polymerases, such as POLK, that incorporate nucleotides opposite lesions and the extender DNA polymerase zeta complex which continues DNA synthesis from…

Subunit structure

Monomer (PubMed:11711549). Homodimer. Homotetramer (By similarity). Interacts (via C-terminal domain) with the DNA polymerase zeta complex which is composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and REV3L forms and stabilizes the DNA polymerase zeta complex before being recruited by REV1 to the DNA lesion site (PubMed:14657033). Forms a quaternary complex with POLK, MAD2L2…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6C8CX-ray1.5 ÅA/B=1150-1249
6C59X-ray2.03 ÅA=1150-1249
4FJOX-ray2.72 ÅA=1153-1249
2LSGNMRA=1150-1249
2LSJNMRA=1135-1249

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