Cell division cycle 5-like protein (CDC5L) is a 802-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99459.
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The mean pLDDT of this model is 74.3 (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 | 24% |
| 70 to 90 | Confident: backbone generally right | 41% |
| 50 to 70 | Low: treat with caution | 19% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:11991638, PubMed:20176811, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30705154, PubMed:30728453). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR) (PubMed:20176811). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs…
Homodimer. Interacts with DAPK3 (By similarity). Component of the precatalytic, catalytic and postcatalytic spliceosome complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30705154, PubMed:30728453). Part of a spliceosomal 'core' complex consisting of CDC5L, PLRG1, SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1,…
Nucleus, Nucleus speckle, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8C6J | EM | 2.8 Å | O=1-802 |
| 6ID1 | EM | 2.86 Å | L=1-802 |
| 7DVQ | EM | 2.89 Å | L=1-802 |
| 6ID0 | EM | 2.9 Å | L=1-802 |
| 6ICZ | EM | 3.0 Å | L=1-802 |
| 8I0R | EM | 3.0 Å | L=1-802 |
| 8I0T | EM | 3.0 Å | L=1-802 |
| 8I0V | EM | 3.0 Å | L=1-802 |
| 7QTT | EM | 3.1 Å | P=1-802 |
| 6QDV | EM | 3.3 Å | O=1-802 |
| 8I0U | EM | 3.3 Å | L=1-802 |
| 9FMD | EM | 3.3 Å | L=1-802 |
| 6ZYM | EM | 3.4 Å | L=1-802 |
| 8I0P | EM | 3.4 Å | L=1-802 |
| 8I0W | EM | 3.4 Å | L=1-802 |
| 8RO2 | EM | 3.5 Å | L=1-802 |
| 5XJC | EM | 3.6 Å | L=1-802 |
| 7W59 | EM | 3.6 Å | L=1-802 |
| 7W5A | EM | 3.6 Å | L=1-802 |
| 5YZG | EM | 4.1 Å | L=1-802 |
Showing 20 of 36 experimental structures (best resolution first).
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