Prelamin-A/C (LMNA) is a 664-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02545.
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The mean pLDDT of this model is 76.4 (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 | 58% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 26% |
What pLDDT means and how to read it
Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly,…
Homodimer of lamin A and lamin C (PubMed:15476822, PubMed:31434876, PubMed:33706103). Lamin dimers then assemble into dimeric head-to-tail polymers (PubMed:31434876). Ultimately, two head-to-tail polymers assemble laterally into a protofilament with a uniformly shaped rod of 3.5 nm in diameter (PubMed:31434876). Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with…
Nucleus lamina, Nucleus envelope, Nucleus, nucleoplasm, Nucleus matrix, Nucleus speckle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7WZZ | X-ray | 1.3 Å | C=490-498 |
| 1IFR | X-ray | 1.4 Å | A=436-552 |
| 7X1B | X-ray | 1.4 Å | C=490-497 |
| 3GEF | X-ray | 1.5 Å | A/B/C/D=436-552 |
| 8I33 | X-ray | 1.62 Å | A/B/C/D=24-65 |
| 7Z21 | X-ray | 1.63 Å | E/F=411-566 |
| 7CRG | X-ray | 1.8 Å | A/B/C=406-553 |
| 7X5D | X-ray | 1.82 Å | A/B=244-339 |
| 6YF5 | X-ray | 1.83 Å | A/B/C/D=17-70 |
| 6GHD | X-ray | 2.1 Å | B/F=428-546 |
| 7YVD | X-ray | 2.1 Å | A/B/C=421-552 |
| 1X8Y | X-ray | 2.2 Å | A=305-387 |
| 6RPR | X-ray | 2.26 Å | B=430-545 |
| 2XV5 | X-ray | 2.4 Å | A/B=328-398 |
| 9UL6 | X-ray | 2.5 Å | A/B/C=406-552 |
| 6SNZ | X-ray | 2.6 Å | A/B/C/D=65-222 |
| 6YSH | X-ray | 2.83 Å | A=25-70, B=26-70 |
| 6YJD | X-ray | 2.9 Å | A=329-403 |
| 3V5B | X-ray | 3.0 Å | A=313-386 |
| 3V4Q | X-ray | 3.06 Å | A=313-386 |
Showing 20 of 28 experimental structures (best resolution first).
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