Structural maintenance of chromosomes protein 1A (SMC1A) is a 1233-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14683.
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The mean pLDDT of this model is 82.8 (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 | 23% |
| 70 to 90 | Confident: backbone generally right | 67% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in…
Forms a heterodimer with SMC3 in cohesin complexes (PubMed:22628566). Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their SMC hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21 (PubMed:11076961, PubMed:22628566, PubMed:32409525). In germ cell cohesin complexes, SMC1A is mutually exclusive…
Nucleus, Chromosome, Chromosome, centromere, kinetochore
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8ROE | X-ray | 1.36 Å | A=1-175, A=1057-1233 |
| 8ROD | X-ray | 1.5 Å | A=1-175, A=1057-1233 |
| 8ROF | X-ray | 1.65 Å | A=1-175, A=1057-1233 |
| 8RO9 | X-ray | 1.77 Å | A/C=1-200, A/C=992-1233 |
| 8ROC | X-ray | 1.85 Å | A=1-175, A=1057-1233 |
| 8RO8 | X-ray | 1.9 Å | A=1-200, A=992-1233 |
| 8ROG | X-ray | 1.94 Å | A=1-175, A=1057-1233 |
| 8RO7 | X-ray | 2.09 Å | A=879-1233 |
| 8RO6 | X-ray | 2.2 Å | A=879-1233 |
| 6WG4 | X-ray | 2.31 Å | A=499-675 |
| 8ROA | X-ray | 2.44 Å | A/C=1-200, A/C=992-1233 |
| 8ROB | X-ray | 2.5 Å | A=1-200, A=992-1233 |
| 6WG6 | X-ray | 3.54 Å | A/C/E/G/I/K=472-702 |
| 8P0A | EM | 3.67 Å | A=1-200, A=992-1233 |
| 6WGE | EM | 3.9 Å | A=1-1233 |
| 8PQ5 | EM | 4.4 Å | A=879-1233 |
| 6WG3 | EM | 5.3 Å | A=1-1233 |
| 7W1M | EM | 6.5 Å | A=1-1233 |
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