DNA replication licensing factor MCM2 (MCM2) is a 904-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P49736.
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The mean pLDDT of this model is 76.3 (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 | 17% |
| 70 to 90 | Confident: backbone generally right | 59% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 14% |
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. 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: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 Walker A box of the adjacent subunit.…
Component of the MCM2-7 complex (PubMed:16899510, PubMed:17296731, PubMed:9305914). The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (PubMed:16899510, PubMed:17296731, PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:9305914). Component of the CMG helicase complex, a hexameric ring of related MCM2-7 subunits stabilized by CDC45…
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6YA7 | X-ray | 1.67 Å | C=33-47 |
| 7CIZ | X-ray | 1.8 Å | C/G/K=61-130 |
| 5BNX | X-ray | 2.31 Å | C=61-130 |
| 5JA4 | X-ray | 2.42 Å | C=61-130 |
| 7CJ0 | X-ray | 2.5 Å | G/H=61-130 |
| 7W1Y | EM | 2.59 Å | 2/A=1-904 |
| 9E2Z | EM | 2.6 Å | 2=1-904 |
| 5BNV | X-ray | 2.79 Å | C/F=61-130 |
| 7PLO | EM | 2.8 Å | 2=1-904 |
| 8W0F | EM | 2.8 Å | 2/A=1-904 |
| 4UUZ | X-ray | 2.9 Å | C=69-138 |
| 5BO0 | X-ray | 2.91 Å | C=61-130 |
| 8S09 | EM | 3.1 Å | 2/A=1-904 |
| 7PFO | EM | 3.2 Å | 2=1-904 |
| 8S0A | EM | 3.2 Å | 2=1-904 |
| 9CAQ | EM | 3.2 Å | 2/A=1-904 |
| 9LXD | EM | 3.27 Å | 2=1-904 |
| 6XTX | EM | 3.29 Å | 2=1-904 |
| 8B9D | EM | 3.4 Å | 2=1-904 |
| 8W0E | EM | 3.4 Å | 2=1-904 |
Showing 20 of 35 experimental structures (best resolution first).
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