Elongin-B (ELOB) is a 118-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15370.
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The mean pLDDT of this model is 92.5 (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 | 88% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed:7638163). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity)
Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC subunit (PubMed:10205047, PubMed:17997974). The elongin BC complex interacts with EPOP; leading to recruit the elongin BC complex to Polycomb group (PcG) target genes, thereby restricting excessive activity of the PRC2/EED-EZH2 complex (By similarity). Component of multiple cullin-RING E3 ubiquitin-protein ligase complexes composed of…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7Z76 | X-ray | 1.32 Å | A=1-104 |
| 9GIO | X-ray | 1.49 Å | A=1-104 |
| 7JTO | X-ray | 1.7 Å | J=1-104 |
| 8BDS | X-ray | 1.72 Å | A=1-104 |
| 4AJY | X-ray | 1.73 Å | B=1-118 |
| 6GMR | X-ray | 1.75 Å | B=1-118 |
| 6HR2 | X-ray | 1.76 Å | D/H=1-104 |
| 7ZLM | X-ray | 1.79 Å | B/E/H/K=1-118 |
| 6I7Q | X-ray | 1.8 Å | B=1-118 |
| 8BB3 | X-ray | 1.8 Å | J=1-104 |
| 6GFX | X-ray | 1.83 Å | A=1-104 |
| 1LM8 | X-ray | 1.85 Å | B=1-118 |
| 9D1Z | X-ray | 1.88 Å | B=1-104 |
| 2C9W | X-ray | 1.9 Å | B=1-118 |
| 6ZHC | X-ray | 1.92 Å | BBB=1-107 |
| 7ZLS | X-ray | 1.92 Å | B/E/H/K=1-118 |
| 6GMN | X-ray | 1.94 Å | A/D/G/J=1-104 |
| 7ZLP | X-ray | 1.94 Å | B=1-118 |
| 6I7R | X-ray | 1.95 Å | B=1-118 |
| 7Z77 | X-ray | 1.97 Å | A=1-104 |
Showing 20 of 227 experimental structures (best resolution first).
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