DNA dC->dU-editing enzyme APOBEC-3G (APOBEC3G) is a 384-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HC16.
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The mean pLDDT of this model is 88.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 66% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms (PubMed:12808465, PubMed:16527742, PubMed:17121840, PubMed:18288108, PubMed:18849968, PubMed:19153609, PubMed:21123384, PubMed:22791714, PubMed:25542899). Exhibits potent antiviral activity against Vif-deficient HIV-1 (PubMed:12167863, PubMed:12859895, PubMed:14557625, PubMed:20219927, PubMed:21835787, PubMed:22807680, PubMed:22915799, PubMed:23097438, PubMed:23152537, PubMed:31397674). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce…
Homodimer (PubMed:11863358, PubMed:17020885, PubMed:18842592, PubMed:25542899). Homooligomer (PubMed:11863358, PubMed:17020885, PubMed:18842592). Can bind RNA to form ribonucleoprotein complexes of high-molecular-mass (HMM) or low-molecular-mass (LMM) (PubMed:11863358, PubMed:17020885, PubMed:18842592). HMM is inactive and heterogeneous in protein composition because of binding nonselectively to…
Cytoplasm, Nucleus, Cytoplasm, P-body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3V4K | X-ray | 1.38 Å | A/B=191-380 |
| 7UXD | X-ray | 1.5 Å | A=191-384 |
| 4ROW | X-ray | 1.7 Å | A=193-384 |
| 4ROV | X-ray | 1.8 Å | A/B=193-384 |
| 6BUX | X-ray | 1.86 Å | A=191-384 |
| 5ZVB | X-ray | 2.0 Å | A/B=198-221 |
| 3V4J | X-ray | 2.04 Å | A/B=191-384 |
| 3IR2 | X-ray | 2.25 Å | A/B=191-384 |
| 3E1U | X-ray | 2.3 Å | A=197-380 |
| 3IQS | X-ray | 2.3 Å | A=197-380 |
| 5ZVA | X-ray | 2.3 Å | A/B=197-221 |
| 8J62 | EM | 2.5 Å | A/B=11-384 |
| 8CX0 | EM | 2.7 Å | A=1-384 |
| 8H0I | EM | 2.8 Å | A/B=11-384 |
| 6BWY | X-ray | 2.9 Å | A/B/E/G=195-384 |
| 8CX2 | EM | 3.2 Å | A/F=1-384 |
| 8CX1 | EM | 3.3 Å | A/F=1-384 |
| 2JYW | NMR | A=198-384 | |
| 2KBO | NMR | A=193-384 | |
| 2KEM | NMR | A=191-384 |
Showing 20 of 22 experimental structures (best resolution first).
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