Baculoviral IAP repeat-containing protein 5 (BIRC5) is a 142-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15392.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 94.8 (very high 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 | 91% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:20627126, PubMed:21364656, PubMed:25778398, PubMed:28218735, PubMed:9859993). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:16322459). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (PubMed:20826784). Involved in the recruitment of CPC to…
Monomer or homodimer. Exists as a homodimer in the apo state and as a monomer in the CPC-bound state. The monomer protects cells against apoptosis more efficiently than the dimer. Only the dimeric form is capable of enhancing tubulin stability in cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex binds pro-CASP9, as well as active CASP9, but much less efficiently.…
Cytoplasm, Nucleus, Chromosome, Chromosome, centromere, Cytoplasm, cytoskeleton, spindle, Chromosome, centromere, kinetochore, Midbody
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2QFA | X-ray | 1.4 Å | A=1-142 |
| 9TPI | X-ray | 1.8 Å | A/B=2-122 |
| 6YIF | X-ray | 1.81 Å | A=1-142 |
| 9TPH | X-ray | 2.0 Å | A/B=2-127 |
| 3UEC | X-ray | 2.18 Å | A=1-142 |
| 2RAW | X-ray | 2.4 Å | A=1-142 |
| 3UIG | X-ray | 2.4 Å | A/B=1-142 |
| 3UIH | X-ray | 2.4 Å | A/B=1-142 |
| 8RUP | EM | 2.42 Å | K=1-142 |
| 3UEF | X-ray | 2.45 Å | A/C=1-142 |
| 7LBO | X-ray | 2.5 Å | A/B=1-142 |
| 6YIH | X-ray | 2.55 Å | A=1-142 |
| 1F3H | X-ray | 2.58 Å | A/B=1-142 |
| 3UEH | X-ray | 2.6 Å | A/B=1-142 |
| 3UII | X-ray | 2.6 Å | A/B=1-142 |
| 4A0I | X-ray | 2.6 Å | A/B=1-142 |
| 7LBP | X-ray | 2.6 Å | A/C=1-142 |
| 3UEE | X-ray | 2.61 Å | A/C=1-142 |
| 7LBQ | X-ray | 2.69 Å | A=1-142 |
| 3UED | X-ray | 2.7 Å | A/C=1-142 |
Showing 20 of 36 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.