DNA repair protein REV1 (REV1) is a 1251-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBZ9.
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The mean pLDDT of this model is 66.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 39% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 41% |
What pLDDT means and how to read it
Bifunctional protein involved in the maintenance of genome stability through translesion DNA synthesis (TLS) and antibody diversification via somatic hypermutation (PubMed:16263170, PubMed:23143872). 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:23143872). 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 distorted primer termini…
Monomer (By similarity). Homodimer (PubMed:23143872). Homotetramer (PubMed:19464298). 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:11485998, PubMed:12529368,…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4EXT | X-ray | 1.9 Å | A=1156-1251 |
| 6WS0 | X-ray | 2.24 Å | HHH=1158-1251 |
| 6ASR | X-ray | 2.36 Å | B=998-1040 |
| 6WS5 | X-ray | 2.47 Å | HHH=1158-1251 |
| 3GQC | X-ray | 2.5 Å | A/B/C/D=330-833 |
| 4GK0 | X-ray | 2.7 Å | E/F=1117-1251 |
| 9VGW | X-ray | 2.7 Å | X/Y/Z=1108-1120 |
| 4BA9 | X-ray | 2.73 Å | A/B/C/D/E/F=1158-1242 |
| 3VU7 | X-ray | 2.8 Å | H=1140-1251 |
| 4GK5 | X-ray | 3.21 Å | E/F=1117-1251 |
| 2EBW | NMR | A=44-133 | |
| 2LSI | NMR | A=1156-1251 | |
| 2LSK | NMR | A=1158-1251 | |
| 2LSY | NMR | A=1158-1251 | |
| 2N1G | NMR | A=1158-1251 | |
| 5VZM | NMR | B=933-1040 | |
| 6AXD | NMR | A=998-1040 |
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