Cleavage and polyadenylation specificity factor subunit 5 (NUDT21) is a 227-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43809.
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The mean pLDDT of this model is 90.4 (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 | 78% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:17024186, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable…
Homodimer (via N- and C-terminus); binds RNA as homodimer (PubMed:18445629, PubMed:20479262, PubMed:20695905). Component of the cleavage factor Im (CFIm) complex which is a heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or a heterodimer of CPSF6 and CPSF7 (PubMed:14561889, PubMed:20695905, PubMed:21295486, PubMed:23187700, PubMed:8626397,…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5R4Q | X-ray | 1.49 Å | A/B=33-227 |
| 5R4R | X-ray | 1.5 Å | A/B=33-227 |
| 5R67 | X-ray | 1.52 Å | A/B=33-227 |
| 5R4S | X-ray | 1.61 Å | A/B=33-227 |
| 5R4T | X-ray | 1.68 Å | A/B=33-227 |
| 5R4P | X-ray | 1.78 Å | A/B=33-227 |
| 3BHO | X-ray | 1.8 Å | A=20-227 |
| 5R64 | X-ray | 1.84 Å | A/B=33-227 |
| 3BAP | X-ray | 1.85 Å | A=1-227 |
| 2CL3 | X-ray | 1.9 Å | A=19-227 |
| 3N9U | X-ray | 1.92 Å | A/B=21-227 |
| 5R4U | X-ray | 1.92 Å | A/B=33-227 |
| 5R66 | X-ray | 2.02 Å | A/B=33-227 |
| 3MDI | X-ray | 2.07 Å | A/B=1-227 |
| 3MDG | X-ray | 2.22 Å | A/B=1-227 |
| 5R65 | X-ray | 2.28 Å | A/B=33-227 |
| 2J8Q | X-ray | 2.3 Å | A/B=20-227 |
| 3P5T | X-ray | 2.7 Å | A/B/C/D/E/F=34-227 |
| 3P6Y | X-ray | 2.9 Å | A/B/E/F/I/J/M/N=34-227 |
| 3Q2S | X-ray | 2.9 Å | A/B=21-227 |
Showing 20 of 21 experimental structures (best resolution first).
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