DNA replication licensing factor MCM5 (MCM5) is a 734-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P33992.
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The mean pLDDT of this model is 78.1 (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 | 10% |
| 70 to 90 | Confident: backbone generally right | 71% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells (PubMed:40940420). Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:16899510, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the…
Component of the MCM2-7 complex (PubMed:16899510, PubMed:17296731). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:16899510, PubMed:17296731, PubMed:32453425). Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS complex (PubMed:32453425, PubMed:34694004,…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7W1Y | EM | 2.59 Å | 5/D=1-734 |
| 9E2Z | EM | 2.6 Å | 5=1-734 |
| 7PLO | EM | 2.8 Å | 5=1-734 |
| 8W0F | EM | 2.8 Å | 5/D=1-734 |
| 8S09 | EM | 3.1 Å | 5/D=1-734 |
| 7PFO | EM | 3.2 Å | 5=1-734 |
| 8S0A | EM | 3.2 Å | 5=1-734 |
| 9CAQ | EM | 3.2 Å | 5/D=1-734 |
| 9LXD | EM | 3.27 Å | 5=1-734 |
| 6XTX | EM | 3.29 Å | 5=1-734 |
| 8B9D | EM | 3.4 Å | 5=1-734 |
| 8W0E | EM | 3.4 Å | 5=1-734 |
| 8W0I | EM | 3.5 Å | 5=1-734 |
| 8S0B | EM | 3.6 Å | 5=1-734 |
| 8S0D | EM | 3.6 Å | 5=1-734 |
| 8S0E | EM | 3.8 Å | 5=1-734 |
| 8W0G | EM | 3.8 Å | 5/D=1-734 |
| 9LXF | EM | 3.86 Å | 5/H=1-734 |
| 9LXE | EM | 3.96 Å | 5/H=1-734 |
| 8S0F | EM | 4.1 Å | 5=1-734 |
Showing 20 of 23 experimental structures (best resolution first).
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