Tumor susceptibility gene 101 protein (TSG101) is a 390-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99816.
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The mean pLDDT of this model is 82.9 (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 | 67% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP,…
Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry (PubMed:18005716). Interacts with VPS37A, VPS37B and VPS37C (PubMed:15218037, PubMed:15509564). Interacts with DMAP1 (PubMed:10888872). Interacts with ubiquitin (PubMed:11595185). Interacts with…
Cytoplasm, Early endosome membrane, Late endosome membrane, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Midbody, Midbody ring, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3OBQ | X-ray | 1.4 Å | A=2-145 |
| 7NLC | X-ray | 1.4 Å | A=1-145 |
| 3OBS | X-ray | 1.5 Å | A=2-145 |
| 3OBU | X-ray | 1.6 Å | A=2-145 |
| 3OBX | X-ray | 1.6 Å | A=2-145 |
| 3P9G | X-ray | 1.8 Å | A=2-145 |
| 3P9H | X-ray | 1.8 Å | A=2-145 |
| 1S1Q | X-ray | 2.0 Å | A/C=1-145 |
| 4YC1 | X-ray | 2.0 Å | A/B/C=1-145 |
| 6VME | X-ray | 2.19 Å | B/F/G/H/I/J=308-388 |
| 4EJE | X-ray | 2.2 Å | A/B=1-145 |
| 7ZLX | X-ray | 2.25 Å | A/B/C/D/E/F/G/H/I/J/K/L=1-145 |
| 2F0R | X-ray | 2.26 Å | A/B=1-145 |
| 4ZNY | X-ray | 2.4 Å | A=4-145 |
| 3IV1 | X-ray | 2.5 Å | A/B/C/D/E/F/G/H=229-304 |
| 1KPP | NMR | A=1-145 | |
| 1KPQ | NMR | A=1-145 | |
| 1M4P | NMR | A=1-145 | |
| 1M4Q | NMR | A=1-145 | |
| 5VKG | NMR | A=1-145 |
Showing 20 of 21 experimental structures (best resolution first).
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