Sister chromatid cohesion protein 1 (MCD1) is a 566-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12158.
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The mean pLDDT of this model is 57.8 (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 | 6% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 20% |
| Below 50 | Very low: often disordered regions | 49% |
What pLDDT means and how to read it
Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. 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 metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate
Interacts directly with IRR1/SCC3 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes
Nucleus, Chromosome, Chromosome, centromere
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6QPQ | X-ray | 2.1 Å | B/D=1-566 |
| 1W1W | X-ray | 2.9 Å | E/F/G/H=451-564 |
| 5FRP | X-ray | 2.9 Å | C/D=116-159 |
| 4UX3 | X-ray | 3.3 Å | B=1-115 |
| 6QPW | EM | 3.3 Å | B=480-564, E=1-160 |
| 6ZZ6 | EM | 3.4 Å | C=67-555 |
| 6H8Q | X-ray | 3.63 Å | G/H=301-400 |
| 5FRS | X-ray | 4.07 Å | C=126-142 |
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