Double-strand-break repair protein rad21 homolog (RAD21) is a 631-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60216.
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The mean pLDDT of this model is 61.2 (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 | 20% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 16% |
| Below 50 | Very low: often disordered regions | 47% |
What pLDDT means and how to read it
As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetitive regions (PubMed:11509732). The cohesin complex may also play a role in spindle pole assembly during mitosis (PubMed:11590136). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (By similarity). May control RUNX1 gene expression (Probable). Binds to and represses APOB gene promoter (PubMed:25575569). May play a role…
Component of the cohesin complex, which consists of an SMC1A/B and SMC3 heterodimer core and 2 non-Smc subunits RAD21 and STAG1/SA1, STAG2/SA2 or STAG3/SA3 (PubMed:10931856, PubMed:11590136, PubMed:22628566, PubMed:25575569, PubMed:32409525). Interacts (via C-terminus) with SMC1A and (via N-terminus) with SMC3; these interactions are direct (PubMed:12198550, PubMed:32409525). The cohesin complex…
Nucleus, Nucleus matrix, Chromosome, Chromosome, centromere, Cytoplasm, cytoskeleton, spindle pole, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8ROE | X-ray | 1.36 Å | B=558-629 |
| 8ROD | X-ray | 1.5 Å | B=558-629 |
| 8ROF | X-ray | 1.65 Å | B=558-629 |
| 8RO9 | X-ray | 1.77 Å | B/D=558-629 |
| 8ROC | X-ray | 1.85 Å | B=558-629 |
| 8RO8 | X-ray | 1.9 Å | B=558-629 |
| 8ROG | X-ray | 1.94 Å | B=558-629 |
| 8RO7 | X-ray | 2.09 Å | B=558-629 |
| 8RO6 | X-ray | 2.2 Å | B=558-629 |
| 8ROK | X-ray | 2.25 Å | B/D=1-102 |
| 6RRC | X-ray | 2.37 Å | B/D=321-345 |
| 8ROA | X-ray | 2.44 Å | B/D=558-629 |
| 8ROI | X-ray | 2.45 Å | B=1-102 |
| 8ROB | X-ray | 2.5 Å | B=558-629 |
| 8ROH | X-ray | 2.6 Å | B=1-102 |
| 6QNX | X-ray | 2.7 Å | B=281-420 |
| 9HN0 | EM | 2.8 Å | A=310-550 |
| 4PJW | X-ray | 2.85 Å | B=281-420 |
| 9HMV | EM | 2.9 Å | B=310-550 |
| 9HN4 | EM | 2.93 Å | A=310-550 |
Showing 20 of 36 experimental structures (best resolution first).
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