Transcription elongation factor SPT5 (SUPT5H) is a 1087-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00267.
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The mean pLDDT of this model is 68.6 (low 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 | 36% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 38% |
What pLDDT means and how to read it
Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A (PubMed:10075709, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF also…
Interacts with SUPT4H1 to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II (Pol II); forms DNA and RNA clamps that stabilize Pol II elongation complex while maintaining the nontemplate DNA strand in the transcription bubble and nascent RNA in the…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5OHQ | X-ray | 1.1 Å | A=979-1087 |
| 3H7H | X-ray | 1.55 Å | B=176-273 |
| 5OHO | X-ray | 1.6 Å | A/B=536-646 |
| 5U98 | X-ray | 2.0 Å | C/F=980-988 |
| 9HVQ | EM | 2.0 Å | Z=1-1087 |
| 9MLC | EM | 2.4 Å | Z=1-1087 |
| 4L1U | X-ray | 2.42 Å | G/H/I/J=778-790 |
| 8UHG | EM | 2.7 Å | Z=1-1087 |
| 8UI0 | EM | 2.7 Å | Z=1-1087 |
| 8UHD | EM | 2.8 Å | Z=1-1087 |
| 9EGX | EM | 2.9 Å | Z=1-1087 |
| 9EGY | EM | 2.9 Å | Z=1-1087 |
| 9EGZ | EM | 2.9 Å | Z=1-1087 |
| 7OL0 | EM | 3.0 Å | Z=1-1087 |
| 7UNC | EM | 3.0 Å | Z=1-1087 |
| 7UND | EM | 3.0 Å | Z=1-1087 |
| 6GMH | EM | 3.1 Å | Z=1-1087 |
| 6TED | EM | 3.1 Å | Z=1-1087 |
| 9EH2 | EM | 3.1 Å | Z=1-1087 |
| 9G0A | EM | 3.1 Å | Z=1-1087 |
Showing 20 of 55 experimental structures (best resolution first).
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