Baculoviral IAP repeat-containing protein 2 (BIRC2) is a 618-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13490.
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The mean pLDDT of this model is 76.6 (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 | 40% |
| 70 to 90 | Confident: backbone generally right | 35% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 20% |
What pLDDT means and how to read it
Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1,…
Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2; the interaction is required for IKBKE ubiquitination. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19. HSP90AB1 (PubMed:25486457). Interacts with UBXN1 (PubMed:25681446). Interacts with GSK3B…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4HY4 | X-ray | 1.25 Å | A/B=260-352 |
| 7QGJ | X-ray | 1.3 Å | A/B=175-256 |
| 3D9T | X-ray | 1.5 Å | A/B=260-352 |
| 8DSF | X-ray | 1.5 Å | A/B/C/D=260-352 |
| 4KMN | X-ray | 1.52 Å | A=260-357 |
| 4LGE | X-ray | 1.55 Å | A/B=260-352 |
| 6HPR | X-ray | 1.7 Å | A=556-618 |
| 7TRL | X-ray | 1.74 Å | A=261-346 |
| 4HY5 | X-ray | 1.75 Å | A/B=238-352 |
| 3UW4 | X-ray | 1.79 Å | A=266-343 |
| 4MU7 | X-ray | 1.79 Å | A/B=260-352 |
| 5M6N | X-ray | 1.8 Å | A/B=266-363 |
| 9N23 | X-ray | 1.8 Å | A/B=260-352 |
| 3T6P | X-ray | 1.9 Å | A=265-618 |
| 3M1D | X-ray | 2.0 Å | A/B=40-119 |
| 4LGU | X-ray | 2.0 Å | A/B=260-352 |
| 6W74 | X-ray | 2.11 Å | A=260-352 |
| 4MTI | X-ray | 2.15 Å | A/B=260-352 |
| 6W7O | X-ray | 2.17 Å | C/D=260-352 |
| 6EXW | X-ray | 2.2 Å | A/C=251-363 |
Showing 20 of 29 experimental structures (best resolution first).
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