E3 ubiquitin-protein ligase XIAP (XIAP) is a 497-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P98170.
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The mean pLDDT of this model is 74.3 (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 | 31% |
| 70 to 90 | Confident: backbone generally right | 38% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 22% |
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, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis (PubMed:11257230, PubMed:11257231, PubMed:11447297, PubMed:12121969, PubMed:12620238, PubMed:17560374, PubMed:17967870, PubMed:19473982, PubMed:20154138, PubMed:22103349, PubMed:9230442). Acts as a direct caspase inhibitor (PubMed:11257230, PubMed:11257231, PubMed:12620238). Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry (PubMed:11257230, PubMed:11257231, PubMed:16352606, PubMed:16916640). Inactivates CASP9 by…
Monomer, and homodimer. Part of a complex composed of SEPTIN4 isoform ARTS, XIAP and BCL2, within the complex interacts with SEPTIN4 isoform ARTS and BCL2, SEPTIN4 isoform ARTS acts as a scaffold protein and stabilizes the complex (PubMed:29020630). Interacts (via BIR3 domain) with DIABLO/SMAC; the interaction inhibits apoptotic suppressor activity (PubMed:11140637, PubMed:11257230,…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4J44 | X-ray | 1.3 Å | A/C=152-236 |
| 8W59 | X-ray | 1.34 Å | A/B=434-496 |
| 4J47 | X-ray | 1.35 Å | A/C=152-236 |
| 4J46 | X-ray | 1.42 Å | A/C=152-236 |
| 4J3Y | X-ray | 1.45 Å | A/C=152-236 |
| 4J45 | X-ray | 1.48 Å | A/C=152-236 |
| 5O6T | X-ray | 1.57 Å | A/B=434-497 |
| 4KJU | X-ray | 1.6 Å | A/C=152-236 |
| 8W5A | X-ray | 1.65 Å | A/B=434-497 |
| 4KJV | X-ray | 1.7 Å | A/C=152-236 |
| 3UW5 | X-ray | 1.71 Å | A/B=336-348 |
| 8GH7 | X-ray | 1.75 Å | A/B=253-347 |
| 4IC3 | X-ray | 1.78 Å | A/B=429-497 |
| 3UW4 | X-ray | 1.79 Å | A=338-348 |
| 2POI | X-ray | 1.8 Å | A=10-99 |
| 3HL5 | X-ray | 1.8 Å | A/B=256-346 |
| 6GJW | X-ray | 1.9 Å | A/B/C/D=10-99 |
| 4KMP | X-ray | 1.95 Å | A/B=256-348 |
| 4WVT | X-ray | 1.96 Å | A/B=156-231 |
| 1G73 | X-ray | 2.0 Å | C/D=238-358 |
Showing 20 of 74 experimental structures (best resolution first).
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